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Iron in PDB 3lgq: Structure of the Thioalkalivibrio Nitratireducens Cytochrome C Nitrite Reductase in Complex with Sulfite (Modified Tyr-303)

Protein crystallography data

The structure of Structure of the Thioalkalivibrio Nitratireducens Cytochrome C Nitrite Reductase in Complex with Sulfite (Modified Tyr-303), PDB code: 3lgq was solved by A.A.Trofimov, K.M.Polyakov, K.M.Boyko, A.A.Filimonenkov, T.V.Tikhonova, V.S.Lamzin, G.P.Bourenkov, V.O.Popov, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.80 / 1.80
Space group P 21 3
Cell size a, b, c (Å), α, β, γ (°) 195.690, 195.690, 195.690, 90.00, 90.00, 90.00
R / Rfree (%) 15 / 16.8

Other elements in 3lgq:

The structure of Structure of the Thioalkalivibrio Nitratireducens Cytochrome C Nitrite Reductase in Complex with Sulfite (Modified Tyr-303) also contains other interesting chemical elements:

Calcium (Ca) 2 atoms

Iron Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 16;

Binding sites:

The binding sites of Iron atom in the Structure of the Thioalkalivibrio Nitratireducens Cytochrome C Nitrite Reductase in Complex with Sulfite (Modified Tyr-303) (pdb code 3lgq). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 16 binding sites of Iron where determined in the Structure of the Thioalkalivibrio Nitratireducens Cytochrome C Nitrite Reductase in Complex with Sulfite (Modified Tyr-303), PDB code: 3lgq:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 16 in 3lgq

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Iron binding site 1 out of 16 in the Structure of the Thioalkalivibrio Nitratireducens Cytochrome C Nitrite Reductase in Complex with Sulfite (Modified Tyr-303)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of the Thioalkalivibrio Nitratireducens Cytochrome C Nitrite Reductase in Complex with Sulfite (Modified Tyr-303) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1004

b:19.9
occ:1.00
FE A:HEC1004 0.0 19.9 1.0
NZ A:LYS188 1.9 22.5 1.0
NA A:HEC1004 2.0 19.3 1.0
NC A:HEC1004 2.0 19.3 1.0
NB A:HEC1004 2.0 20.2 1.0
ND A:HEC1004 2.1 19.5 1.0
S A:SO3526 2.3 24.2 1.0
C1C A:HEC1004 3.0 19.7 1.0
C1A A:HEC1004 3.0 20.9 1.0
C4A A:HEC1004 3.0 20.3 1.0
C4B A:HEC1004 3.1 20.3 1.0
CE A:LYS188 3.1 22.4 1.0
C4D A:HEC1004 3.1 19.3 1.0
C4C A:HEC1004 3.1 20.1 1.0
C1B A:HEC1004 3.1 20.2 1.0
O2 A:SO3526 3.1 27.9 1.0
C1D A:HEC1004 3.1 19.8 1.0
O1 A:SO3526 3.1 26.5 1.0
O3 A:SO3526 3.2 23.4 1.0
CHC A:HEC1004 3.4 21.3 1.0
CHA A:HEC1004 3.4 20.1 1.0
CHB A:HEC1004 3.5 20.0 1.0
CHD A:HEC1004 3.5 19.3 1.0
C3A A:HEC1004 4.2 19.2 1.0
C2A A:HEC1004 4.2 19.2 1.0
C2C A:HEC1004 4.3 18.3 1.0
C2B A:HEC1004 4.3 22.1 1.0
C3C A:HEC1004 4.3 18.1 1.0
C3B A:HEC1004 4.3 22.0 1.0
C3D A:HEC1004 4.3 18.9 1.0
C2D A:HEC1004 4.3 18.1 1.0
CD A:LYS188 4.5 20.6 1.0
NE2 A:HIS361 4.5 20.1 1.0
O A:HOH727 4.6 24.1 1.0
NH2 A:ARG131 4.9 20.1 1.0
CMD A:HEC1006 4.9 17.7 1.0
O A:HOH717 5.0 25.4 1.0

Iron binding site 2 out of 16 in 3lgq

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Iron binding site 2 out of 16 in the Structure of the Thioalkalivibrio Nitratireducens Cytochrome C Nitrite Reductase in Complex with Sulfite (Modified Tyr-303)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of the Thioalkalivibrio Nitratireducens Cytochrome C Nitrite Reductase in Complex with Sulfite (Modified Tyr-303) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1005

b:19.1
occ:1.00
FE A:HEC1005 0.0 19.1 1.0
NE2 A:HIS231 2.0 19.7 1.0
NE2 A:HIS398 2.0 17.7 1.0
NC A:HEC1005 2.0 18.2 1.0
NA A:HEC1005 2.0 18.5 1.0
ND A:HEC1005 2.0 19.6 1.0
NB A:HEC1005 2.1 18.9 1.0
CE1 A:HIS231 2.9 21.8 1.0
CD2 A:HIS398 2.9 18.3 1.0
CD2 A:HIS231 3.0 21.3 1.0
CE1 A:HIS398 3.0 21.8 1.0
C1D A:HEC1005 3.0 19.1 1.0
C1A A:HEC1005 3.0 17.4 1.0
C4D A:HEC1005 3.0 18.8 1.0
C4C A:HEC1005 3.0 18.9 1.0
C1C A:HEC1005 3.0 17.8 1.0
C4A A:HEC1005 3.1 17.1 1.0
C1B A:HEC1005 3.1 18.5 1.0
C4B A:HEC1005 3.1 16.8 1.0
CHD A:HEC1005 3.4 19.6 1.0
CHA A:HEC1005 3.4 17.4 1.0
CHC A:HEC1005 3.4 17.1 1.0
CHB A:HEC1005 3.5 18.1 1.0
ND1 A:HIS231 4.0 20.3 1.0
ND1 A:HIS398 4.1 20.5 1.0
CG A:HIS398 4.1 20.0 1.0
CG A:HIS231 4.1 21.1 1.0
C2A A:HEC1005 4.3 18.0 1.0
C3D A:HEC1005 4.3 18.8 1.0
C3A A:HEC1005 4.3 18.5 1.0
C2D A:HEC1005 4.3 19.2 1.0
C2C A:HEC1005 4.3 17.9 1.0
C2B A:HEC1005 4.3 18.8 1.0
C3C A:HEC1005 4.3 19.2 1.0
C3B A:HEC1005 4.3 19.1 1.0

Iron binding site 3 out of 16 in 3lgq

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Iron binding site 3 out of 16 in the Structure of the Thioalkalivibrio Nitratireducens Cytochrome C Nitrite Reductase in Complex with Sulfite (Modified Tyr-303)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Structure of the Thioalkalivibrio Nitratireducens Cytochrome C Nitrite Reductase in Complex with Sulfite (Modified Tyr-303) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1006

b:18.8
occ:1.00
FE A:HEC1006 0.0 18.8 1.0
NE2 A:HIS300 1.9 18.9 1.0
NE2 A:HIS119 2.0 19.7 1.0
NB A:HEC1006 2.0 18.5 1.0
ND A:HEC1006 2.0 19.5 1.0
NC A:HEC1006 2.1 19.0 1.0
NA A:HEC1006 2.1 17.4 1.0
CE1 A:HIS119 2.9 17.6 1.0
CE1 A:HIS300 2.9 20.5 1.0
CD2 A:HIS300 3.0 20.1 1.0
C1B A:HEC1006 3.0 19.9 1.0
CD2 A:HIS119 3.0 18.9 1.0
C1D A:HEC1006 3.1 18.8 1.0
C4C A:HEC1006 3.1 18.4 1.0
C4B A:HEC1006 3.1 20.1 1.0
C4D A:HEC1006 3.1 18.6 1.0
C4A A:HEC1006 3.1 18.9 1.0
C1C A:HEC1006 3.1 20.1 1.0
C1A A:HEC1006 3.1 18.4 1.0
CHD A:HEC1006 3.4 17.3 1.0
CHB A:HEC1006 3.4 17.0 1.0
CHA A:HEC1006 3.5 18.5 1.0
CHC A:HEC1006 3.5 18.5 1.0
ND1 A:HIS119 4.0 18.9 1.0
ND1 A:HIS300 4.0 19.9 1.0
CG A:HIS300 4.1 20.2 1.0
CG A:HIS119 4.1 18.6 1.0
C2B A:HEC1006 4.2 20.6 1.0
C3B A:HEC1006 4.3 19.6 1.0
C2C A:HEC1006 4.3 18.1 1.0
C2A A:HEC1006 4.3 18.1 1.0
C3D A:HEC1006 4.3 15.9 1.0
C2D A:HEC1006 4.3 18.1 1.0
C3A A:HEC1006 4.3 17.5 1.0
C3C A:HEC1006 4.3 17.7 1.0

Iron binding site 4 out of 16 in 3lgq

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Iron binding site 4 out of 16 in the Structure of the Thioalkalivibrio Nitratireducens Cytochrome C Nitrite Reductase in Complex with Sulfite (Modified Tyr-303)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Structure of the Thioalkalivibrio Nitratireducens Cytochrome C Nitrite Reductase in Complex with Sulfite (Modified Tyr-303) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1007

b:19.6
occ:1.00
FE A:HEC1007 0.0 19.6 1.0
NE2 A:HIS491 1.9 19.0 1.0
NE2 A:HIS383 1.9 20.1 1.0
NA A:HEC1007 2.0 19.1 1.0
NC A:HEC1007 2.0 18.4 1.0
NB A:HEC1007 2.0 19.5 1.0
ND A:HEC1007 2.1 20.4 1.0
CE1 A:HIS491 2.8 20.0 1.0
CE1 A:HIS383 2.9 19.3 1.0
CD2 A:HIS383 3.0 19.2 1.0
C1A A:HEC1007 3.0 19.8 1.0
CD2 A:HIS491 3.0 19.5 1.0
C4D A:HEC1007 3.0 20.1 1.0
C1C A:HEC1007 3.0 20.0 1.0
C4A A:HEC1007 3.0 18.9 1.0
C4B A:HEC1007 3.1 19.1 1.0
C1B A:HEC1007 3.1 19.1 1.0
C4C A:HEC1007 3.1 19.1 1.0
C1D A:HEC1007 3.1 21.2 1.0
CHA A:HEC1007 3.4 19.8 1.0
CHC A:HEC1007 3.4 19.8 1.0
CHB A:HEC1007 3.4 18.9 1.0
CHD A:HEC1007 3.4 18.6 1.0
ND1 A:HIS491 4.0 19.3 1.0
ND1 A:HIS383 4.0 19.5 1.0
CG A:HIS491 4.1 19.4 1.0
CG A:HIS383 4.1 19.4 1.0
C3A A:HEC1007 4.2 19.4 1.0
C2A A:HEC1007 4.2 18.8 1.0
C2C A:HEC1007 4.3 19.2 1.0
C2B A:HEC1007 4.3 20.1 1.0
C3D A:HEC1007 4.3 18.8 1.0
C3C A:HEC1007 4.3 18.5 1.0
C3B A:HEC1007 4.3 19.9 1.0
C2D A:HEC1007 4.3 20.5 1.0

Iron binding site 5 out of 16 in 3lgq

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Iron binding site 5 out of 16 in the Structure of the Thioalkalivibrio Nitratireducens Cytochrome C Nitrite Reductase in Complex with Sulfite (Modified Tyr-303)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Structure of the Thioalkalivibrio Nitratireducens Cytochrome C Nitrite Reductase in Complex with Sulfite (Modified Tyr-303) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1008

b:21.9
occ:1.00
FE A:HEC1008 0.0 21.9 1.0
NE2 A:HIS372 1.9 20.5 1.0
NE2 A:HIS415 1.9 23.6 1.0
NB A:HEC1008 2.0 23.1 1.0
NA A:HEC1008 2.0 22.4 1.0
ND A:HEC1008 2.0 23.4 1.0
NC A:HEC1008 2.1 24.7 1.0
CE1 A:HIS415 2.9 25.4 1.0
CE1 A:HIS372 2.9 22.8 1.0
CD2 A:HIS372 3.0 22.2 1.0
CD2 A:HIS415 3.0 24.5 1.0
C4B A:HEC1008 3.0 23.7 1.0
C1B A:HEC1008 3.0 21.2 1.0
C1A A:HEC1008 3.0 24.5 1.0
C4D A:HEC1008 3.0 26.0 1.0
C1C A:HEC1008 3.1 25.6 1.0
C1D A:HEC1008 3.1 27.1 1.0
C4A A:HEC1008 3.1 22.2 1.0
C4C A:HEC1008 3.1 26.1 1.0
CHA A:HEC1008 3.4 24.7 1.0
CHC A:HEC1008 3.4 24.7 1.0
CHD A:HEC1008 3.4 26.4 1.0
CHB A:HEC1008 3.4 20.4 1.0
ND1 A:HIS372 4.0 22.9 1.0
ND1 A:HIS415 4.0 26.3 1.0
CG A:HIS372 4.1 22.8 1.0
CG A:HIS415 4.1 25.4 1.0
C2B A:HEC1008 4.2 23.2 1.0
C3B A:HEC1008 4.2 22.6 1.0
C2A A:HEC1008 4.3 23.9 1.0
C2C A:HEC1008 4.3 25.7 1.0
C3A A:HEC1008 4.3 22.7 1.0
C3D A:HEC1008 4.3 27.8 1.0
C2D A:HEC1008 4.3 28.5 1.0
C3C A:HEC1008 4.3 27.6 1.0
CBC A:HEC1007 4.9 19.2 1.0

Iron binding site 6 out of 16 in 3lgq

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Iron binding site 6 out of 16 in the Structure of the Thioalkalivibrio Nitratireducens Cytochrome C Nitrite Reductase in Complex with Sulfite (Modified Tyr-303)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Structure of the Thioalkalivibrio Nitratireducens Cytochrome C Nitrite Reductase in Complex with Sulfite (Modified Tyr-303) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1002

b:21.0
occ:1.00
FE A:HEC1002 0.0 21.0 1.0
NE2 A:HIS234 1.9 18.7 1.0
NE2 A:HIS39 1.9 19.1 1.0
NA A:HEC1002 2.0 21.7 1.0
NC A:HEC1002 2.0 19.4 1.0
ND A:HEC1002 2.1 20.7 1.0
NB A:HEC1002 2.1 21.9 1.0
CE1 A:HIS234 2.9 18.9 1.0
CD2 A:HIS39 2.9 19.5 1.0
CE1 A:HIS39 2.9 17.5 1.0
CD2 A:HIS234 3.0 20.0 1.0
C4A A:HEC1002 3.0 22.2 1.0
C4C A:HEC1002 3.0 20.1 1.0
C1B A:HEC1002 3.0 21.7 1.0
C1D A:HEC1002 3.0 21.1 1.0
C1A A:HEC1002 3.1 21.5 1.0
C1C A:HEC1002 3.1 20.6 1.0
C4D A:HEC1002 3.1 21.3 1.0
C4B A:HEC1002 3.1 22.0 1.0
CHB A:HEC1002 3.4 22.2 1.0
CHD A:HEC1002 3.4 19.6 1.0
CHA A:HEC1002 3.5 21.3 1.0
CHC A:HEC1002 3.5 19.9 1.0
ND1 A:HIS234 4.0 19.0 1.0
ND1 A:HIS39 4.1 19.9 1.0
CG A:HIS234 4.1 17.7 1.0
CG A:HIS39 4.1 19.9 1.0
C3A A:HEC1002 4.3 21.6 1.0
C2B A:HEC1002 4.3 23.1 1.0
C2A A:HEC1002 4.3 21.6 1.0
C3C A:HEC1002 4.3 18.8 1.0
C2C A:HEC1002 4.3 20.0 1.0
C2D A:HEC1002 4.3 19.5 1.0
C3B A:HEC1002 4.4 23.0 1.0
C3D A:HEC1002 4.4 19.4 1.0

Iron binding site 7 out of 16 in 3lgq

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Iron binding site 7 out of 16 in the Structure of the Thioalkalivibrio Nitratireducens Cytochrome C Nitrite Reductase in Complex with Sulfite (Modified Tyr-303)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Structure of the Thioalkalivibrio Nitratireducens Cytochrome C Nitrite Reductase in Complex with Sulfite (Modified Tyr-303) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1003

b:19.6
occ:1.00
FE A:HEC1003 0.0 19.6 1.0
NE2 A:HIS30 2.0 21.1 1.0
NB A:HEC1003 2.0 19.6 1.0
NE2 A:HIS70 2.0 19.3 1.0
ND A:HEC1003 2.0 20.2 1.0
NC A:HEC1003 2.0 21.0 1.0
NA A:HEC1003 2.0 20.6 1.0
CE1 A:HIS30 2.9 19.4 1.0
CE1 A:HIS70 2.9 22.5 1.0
CD2 A:HIS70 3.0 20.7 1.0
C1B A:HEC1003 3.0 20.4 1.0
C1D A:HEC1003 3.0 20.7 1.0
CD2 A:HIS30 3.0 20.8 1.0
C4C A:HEC1003 3.0 19.1 1.0
C4B A:HEC1003 3.1 18.9 1.0
C4A A:HEC1003 3.1 19.1 1.0
C1C A:HEC1003 3.1 20.1 1.0
C4D A:HEC1003 3.1 20.2 1.0
C1A A:HEC1003 3.1 18.0 1.0
CHD A:HEC1003 3.4 18.6 1.0
CHB A:HEC1003 3.4 18.5 1.0
CHC A:HEC1003 3.4 19.3 1.0
CHA A:HEC1003 3.5 18.5 1.0
ND1 A:HIS30 4.0 23.3 1.0
ND1 A:HIS70 4.1 19.8 1.0
CG A:HIS70 4.1 17.7 1.0
CG A:HIS30 4.1 21.3 1.0
C2B A:HEC1003 4.2 20.0 1.0
C3B A:HEC1003 4.3 19.7 1.0
C2D A:HEC1003 4.3 21.0 1.0
C3A A:HEC1003 4.3 19.4 1.0
C3C A:HEC1003 4.3 19.9 1.0
C3D A:HEC1003 4.3 22.5 1.0
C2C A:HEC1003 4.3 19.3 1.0
C2A A:HEC1003 4.3 19.3 1.0

Iron binding site 8 out of 16 in 3lgq

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Iron binding site 8 out of 16 in the Structure of the Thioalkalivibrio Nitratireducens Cytochrome C Nitrite Reductase in Complex with Sulfite (Modified Tyr-303)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Structure of the Thioalkalivibrio Nitratireducens Cytochrome C Nitrite Reductase in Complex with Sulfite (Modified Tyr-303) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1001

b:21.6
occ:1.00
FE A:HEC1001 0.0 21.6 1.0
NE2 A:HIS18 1.9 19.7 1.0
NE2 A:HIS44 1.9 22.0 1.0
ND A:HEC1001 2.0 22.9 1.0
NA A:HEC1001 2.1 22.9 1.0
NB A:HEC1001 2.1 23.6 1.0
NC A:HEC1001 2.1 22.5 1.0
CE1 A:HIS18 2.8 21.1 1.0
CE1 A:HIS44 2.9 22.4 1.0
CD2 A:HIS18 3.0 21.4 1.0
CD2 A:HIS44 3.0 22.3 1.0
C1D A:HEC1001 3.0 24.9 1.0
C4A A:HEC1001 3.1 22.9 1.0
C4D A:HEC1001 3.1 23.6 1.0
C4C A:HEC1001 3.1 24.9 1.0
C1B A:HEC1001 3.1 23.3 1.0
C1C A:HEC1001 3.1 22.6 1.0
C1A A:HEC1001 3.1 22.4 1.0
C4B A:HEC1001 3.1 22.8 1.0
CHD A:HEC1001 3.4 24.2 1.0
CHB A:HEC1001 3.4 21.8 1.0
CHA A:HEC1001 3.5 22.8 1.0
CHC A:HEC1001 3.5 23.0 1.0
ND1 A:HIS18 4.0 20.9 1.0
ND1 A:HIS44 4.0 23.7 1.0
CG A:HIS18 4.1 21.3 1.0
CG A:HIS44 4.1 23.5 1.0
C2D A:HEC1001 4.3 24.0 1.0
C3D A:HEC1001 4.3 23.9 1.0
C3A A:HEC1001 4.3 21.8 1.0
C2A A:HEC1001 4.3 19.8 1.0
C2B A:HEC1001 4.3 22.9 1.0
C2C A:HEC1001 4.3 23.6 1.0
C3C A:HEC1001 4.3 22.0 1.0
C3B A:HEC1001 4.4 21.9 1.0
CMA A:HEC1002 4.8 21.2 1.0

Iron binding site 9 out of 16 in 3lgq

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Iron binding site 9 out of 16 in the Structure of the Thioalkalivibrio Nitratireducens Cytochrome C Nitrite Reductase in Complex with Sulfite (Modified Tyr-303)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of Structure of the Thioalkalivibrio Nitratireducens Cytochrome C Nitrite Reductase in Complex with Sulfite (Modified Tyr-303) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe1004

b:18.8
occ:1.00
FE B:HEC1004 0.0 18.8 1.0
NZ B:LYS188 1.9 20.8 1.0
NA B:HEC1004 2.0 17.1 1.0
NC B:HEC1004 2.0 19.3 1.0
ND B:HEC1004 2.0 18.1 1.0
NB B:HEC1004 2.0 18.5 1.0
S B:SO3526 2.3 22.5 1.0
C1A B:HEC1004 3.0 19.8 1.0
C1C B:HEC1004 3.0 19.8 1.0
CE B:LYS188 3.0 21.6 1.0
C4B B:HEC1004 3.0 19.7 1.0
C4D B:HEC1004 3.0 18.7 1.0
C4A B:HEC1004 3.0 17.5 1.0
C4C B:HEC1004 3.1 17.8 1.0
C1D B:HEC1004 3.1 18.8 1.0
O2 B:SO3526 3.1 26.8 1.0
C1B B:HEC1004 3.1 18.8 1.0
O1 B:SO3526 3.2 27.7 1.0
O3 B:SO3526 3.2 21.6 1.0
CHC B:HEC1004 3.4 20.1 1.0
CHA B:HEC1004 3.4 19.3 1.0
CHD B:HEC1004 3.5 18.8 1.0
CHB B:HEC1004 3.5 17.6 1.0
C2A B:HEC1004 4.2 16.6 1.0
C3A B:HEC1004 4.2 18.4 1.0
C2C B:HEC1004 4.3 18.9 1.0
C3C B:HEC1004 4.3 19.0 1.0
C3D B:HEC1004 4.3 18.4 1.0
C3B B:HEC1004 4.3 19.3 1.0
C2D B:HEC1004 4.3 16.8 1.0
C2B B:HEC1004 4.3 19.5 1.0
CD B:LYS188 4.4 19.9 1.0
NE2 B:HIS361 4.5 18.3 1.0
O B:HOH792 4.6 23.9 1.0
CMD B:HEC1006 4.9 15.4 1.0
NH2 B:ARG131 4.9 19.4 1.0

Iron binding site 10 out of 16 in 3lgq

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Iron binding site 10 out of 16 in the Structure of the Thioalkalivibrio Nitratireducens Cytochrome C Nitrite Reductase in Complex with Sulfite (Modified Tyr-303)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of Structure of the Thioalkalivibrio Nitratireducens Cytochrome C Nitrite Reductase in Complex with Sulfite (Modified Tyr-303) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe1005

b:19.1
occ:1.00
FE B:HEC1005 0.0 19.1 1.0
NE2 B:HIS231 2.0 18.7 1.0
NE2 B:HIS398 2.0 18.3 1.0
NA B:HEC1005 2.0 16.9 1.0
NC B:HEC1005 2.0 18.9 1.0
ND B:HEC1005 2.0 19.9 1.0
NB B:HEC1005 2.0 19.4 1.0
CE1 B:HIS231 3.0 20.1 1.0
CD2 B:HIS398 3.0 18.4 1.0
CD2 B:HIS231 3.0 18.5 1.0
CE1 B:HIS398 3.0 21.2 1.0
C4A B:HEC1005 3.0 16.6 1.0
C4D B:HEC1005 3.0 19.7 1.0
C1D B:HEC1005 3.0 18.3 1.0
C1C B:HEC1005 3.0 17.8 1.0
C1A B:HEC1005 3.1 18.4 1.0
C1B B:HEC1005 3.1 17.0 1.0
C4B B:HEC1005 3.1 17.8 1.0
C4C B:HEC1005 3.1 16.2 1.0
CHB B:HEC1005 3.4 16.2 1.0
CHC B:HEC1005 3.4 16.7 1.0
CHD B:HEC1005 3.4 16.8 1.0
CHA B:HEC1005 3.4 17.3 1.0
ND1 B:HIS231 4.1 18.2 1.0
ND1 B:HIS398 4.1 19.7 1.0
CG B:HIS231 4.1 18.3 1.0
CG B:HIS398 4.1 20.0 1.0
C3A B:HEC1005 4.2 19.4 1.0
C2B B:HEC1005 4.2 17.0 1.0
C3D B:HEC1005 4.3 19.6 1.0
C2A B:HEC1005 4.3 19.7 1.0
C2D B:HEC1005 4.3 19.4 1.0
C2C B:HEC1005 4.3 19.3 1.0
C3B B:HEC1005 4.3 16.6 1.0
C3C B:HEC1005 4.3 17.9 1.0

Reference:

A.A.Trofimov, K.M.Polyakov, T.V.Tikhonova, A.V.Tikhonov, T.N.Safonova, K.M.Boyko, P.V.Dorovatovskii, V.O.Popov. Covalent Modifications of the Catalytic Tyrosine in Octahaem Cytochrome C Nitrite Reductase and Their Effect on the Enzyme Activity. Acta Crystallogr.,Sect.D V. 68 144 2012.
ISSN: ISSN 0907-4449
PubMed: 22281743
DOI: 10.1107/S0907444911052632
Page generated: Sun Dec 13 15:11:21 2020

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