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Iron in PDB 7uur: The 1.67 Angstrom Cryoem Structure of the [Nife]-Hydrogenase Huc From Mycobacterium Smegmatis - Catalytic Dimer (HUC2S2L)

Enzymatic activity of The 1.67 Angstrom Cryoem Structure of the [Nife]-Hydrogenase Huc From Mycobacterium Smegmatis - Catalytic Dimer (HUC2S2L)

All present enzymatic activity of The 1.67 Angstrom Cryoem Structure of the [Nife]-Hydrogenase Huc From Mycobacterium Smegmatis - Catalytic Dimer (HUC2S2L):
1.12.99.6;

Other elements in 7uur:

The structure of The 1.67 Angstrom Cryoem Structure of the [Nife]-Hydrogenase Huc From Mycobacterium Smegmatis - Catalytic Dimer (HUC2S2L) also contains other interesting chemical elements:

Nickel (Ni) 2 atoms
Magnesium (Mg) 2 atoms

Iron Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20;

Binding sites:

The binding sites of Iron atom in the The 1.67 Angstrom Cryoem Structure of the [Nife]-Hydrogenase Huc From Mycobacterium Smegmatis - Catalytic Dimer (HUC2S2L) (pdb code 7uur). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 20 binding sites of Iron where determined in the The 1.67 Angstrom Cryoem Structure of the [Nife]-Hydrogenase Huc From Mycobacterium Smegmatis - Catalytic Dimer (HUC2S2L), PDB code: 7uur:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 20 in 7uur

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Iron binding site 1 out of 20 in the The 1.67 Angstrom Cryoem Structure of the [Nife]-Hydrogenase Huc From Mycobacterium Smegmatis - Catalytic Dimer (HUC2S2L)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of The 1.67 Angstrom Cryoem Structure of the [Nife]-Hydrogenase Huc From Mycobacterium Smegmatis - Catalytic Dimer (HUC2S2L) within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe602

b:13.4
occ:1.00
FE C:FCO602 0.0 13.4 1.0
C3 C:FCO602 1.9 13.4 1.0
C1 C:FCO602 1.9 13.4 1.0
C2 C:FCO602 1.9 13.4 1.0
O C:OH603 2.3 20.0 1.0
SG C:CYS65 2.3 9.1 1.0
SG C:CYS513 2.4 10.6 1.0
NI C:3NI601 2.8 38.4 1.0
O3 C:FCO602 2.9 13.4 1.0
N1 C:FCO602 3.0 13.4 1.0
N2 C:FCO602 3.0 13.4 1.0
CB C:CYS65 3.2 9.1 1.0
CB C:CYS513 3.4 10.6 1.0
CD C:ARG443 4.1 11.4 1.0
NE2 C:HIS69 4.2 7.6 1.0
CB C:CYS510 4.3 12.5 1.0
SG C:CYS510 4.4 12.5 1.0
CB C:ALA441 4.5 10.6 1.0
CA C:CYS65 4.6 9.1 1.0
CD C:PRO465 4.6 10.8 1.0
CB C:CYS62 4.6 9.2 1.0
SG C:CYS62 4.6 9.2 1.0
CG C:PRO465 4.6 10.8 1.0
NH1 C:ARG443 4.7 11.4 1.0
CD2 C:HIS69 4.7 7.6 1.0
CA C:CYS513 4.8 10.6 1.0
CB C:ARG443 4.9 11.4 1.0
O C:CYS65 5.0 9.1 1.0
N C:CYS65 5.0 9.1 1.0

Iron binding site 2 out of 20 in 7uur

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Iron binding site 2 out of 20 in the The 1.67 Angstrom Cryoem Structure of the [Nife]-Hydrogenase Huc From Mycobacterium Smegmatis - Catalytic Dimer (HUC2S2L)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of The 1.67 Angstrom Cryoem Structure of the [Nife]-Hydrogenase Huc From Mycobacterium Smegmatis - Catalytic Dimer (HUC2S2L) within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe402

b:10.2
occ:1.00
FE1 D:F3S402 0.0 10.2 1.0
S1 D:F3S402 2.2 10.2 1.0
S2 D:F3S402 2.3 10.2 1.0
S3 D:F3S402 2.3 10.2 1.0
SG D:CYS161 2.3 6.1 1.0
FE4 D:F3S402 2.7 10.2 1.0
FE3 D:F3S402 2.7 10.2 1.0
CB D:CYS161 3.2 6.1 1.0
CA D:CYS161 3.3 6.1 1.0
O D:HOH608 3.4 8.0 1.0
C D:CYS161 3.7 6.1 1.0
CG C:ARG60 4.0 6.8 1.0
S4 D:F3S402 4.0 10.2 1.0
N D:PRO162 4.2 5.9 1.0
O D:CYS161 4.3 6.1 1.0
ND2 D:ASN15 4.3 7.4 1.0
CA D:PRO162 4.4 5.9 1.0
O D:GLY160 4.4 6.6 1.0
SG D:CYS113 4.5 7.3 1.0
NE2 C:DHI166 4.5 6.3 1.0
N D:CYS161 4.6 6.1 1.0
CD2 C:DHI166 4.6 6.3 1.0
SG D:CYS12 4.6 7.8 1.0
NE C:ARG60 4.6 6.8 1.0
CD C:ARG60 4.9 6.8 1.0
C D:GLY160 5.0 6.6 1.0

Iron binding site 3 out of 20 in 7uur

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Iron binding site 3 out of 20 in the The 1.67 Angstrom Cryoem Structure of the [Nife]-Hydrogenase Huc From Mycobacterium Smegmatis - Catalytic Dimer (HUC2S2L)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of The 1.67 Angstrom Cryoem Structure of the [Nife]-Hydrogenase Huc From Mycobacterium Smegmatis - Catalytic Dimer (HUC2S2L) within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe402

b:10.2
occ:1.00
FE3 D:F3S402 0.0 10.2 1.0
S1 D:F3S402 2.2 10.2 1.0
S4 D:F3S402 2.3 10.2 1.0
S3 D:F3S402 2.3 10.2 1.0
SG D:CYS113 2.3 7.3 1.0
FE4 D:F3S402 2.6 10.2 1.0
FE1 D:F3S402 2.7 10.2 1.0
CB D:CYS113 3.0 7.3 1.0
O D:HOH545 3.4 8.0 1.0
O D:HOH608 3.5 8.0 1.0
O D:HOH592 3.8 9.3 1.0
N D:CYS113 3.9 7.3 1.0
S2 D:F3S402 3.9 10.2 1.0
ND2 D:ASN15 4.0 7.4 1.0
CA D:CYS113 4.1 7.3 1.0
SG D:CYS161 4.6 6.1 1.0
N D:CYS12 4.6 7.8 1.0
CA D:GLY73 4.7 8.3 1.0
O D:GLY10 4.8 9.3 1.0
SG D:CYS12 4.8 7.8 1.0
CA D:ALA11 4.8 9.2 1.0
N D:GLY73 4.9 8.3 1.0
N D:ASP112 5.0 6.7 1.0

Iron binding site 4 out of 20 in 7uur

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Iron binding site 4 out of 20 in the The 1.67 Angstrom Cryoem Structure of the [Nife]-Hydrogenase Huc From Mycobacterium Smegmatis - Catalytic Dimer (HUC2S2L)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of The 1.67 Angstrom Cryoem Structure of the [Nife]-Hydrogenase Huc From Mycobacterium Smegmatis - Catalytic Dimer (HUC2S2L) within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe402

b:10.2
occ:1.00
FE4 D:F3S402 0.0 10.2 1.0
S2 D:F3S402 2.3 10.2 1.0
S4 D:F3S402 2.3 10.2 1.0
SG D:CYS12 2.3 7.8 1.0
S3 D:F3S402 2.3 10.2 1.0
FE3 D:F3S402 2.6 10.2 1.0
FE1 D:F3S402 2.7 10.2 1.0
CB D:CYS12 3.4 7.8 1.0
N D:CYS12 3.6 7.8 1.0
S1 D:F3S402 3.7 10.2 1.0
ND2 D:ASN15 3.9 7.4 1.0
N D:GLY14 3.9 7.5 1.0
CA D:CYS12 4.0 7.8 1.0
NE2 C:DHI166 4.2 6.3 1.0
CA D:GLY14 4.3 7.5 1.0
O D:HOH592 4.3 9.3 1.0
C D:CYS12 4.4 7.8 1.0
N D:SER13 4.4 8.5 1.0
CG C:ARG60 4.6 6.8 1.0
SG D:CYS113 4.7 7.3 1.0
N D:ASN15 4.7 7.4 1.0
C D:ALA11 4.8 9.2 1.0
SG D:CYS161 4.8 6.1 1.0
O C:ARG60 4.8 6.8 1.0
OE2 D:GLU72 4.9 8.7 1.0
C D:GLY14 5.0 7.5 1.0

Iron binding site 5 out of 20 in 7uur

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Iron binding site 5 out of 20 in the The 1.67 Angstrom Cryoem Structure of the [Nife]-Hydrogenase Huc From Mycobacterium Smegmatis - Catalytic Dimer (HUC2S2L)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of The 1.67 Angstrom Cryoem Structure of the [Nife]-Hydrogenase Huc From Mycobacterium Smegmatis - Catalytic Dimer (HUC2S2L) within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe403

b:8.8
occ:1.00
FE1 D:F3S403 0.0 8.8 1.0
S1 D:F3S403 2.2 8.8 1.0
S2 D:F3S403 2.3 8.8 1.0
SG D:CYS260 2.3 5.9 1.0
S3 D:F3S403 2.3 8.8 1.0
FE4 D:F3S403 2.7 8.8 1.0
FE3 D:F3S403 2.7 8.8 1.0
CB D:CYS260 3.2 5.9 1.0
CA D:CYS260 3.6 5.9 1.0
OG1 D:THR199 3.7 5.6 1.0
N D:LEU261 3.8 6.3 1.0
N D:GLY262 3.8 7.0 1.0
S4 D:F3S403 4.0 8.8 1.0
C D:CYS260 4.0 5.9 1.0
CG2 D:THR199 4.1 5.6 1.0
N D:CYS263 4.2 6.2 1.0
CA D:GLY262 4.4 7.0 1.0
CB D:THR199 4.4 5.6 1.0
NZ D:LYS253 4.5 4.9 1.0
CD D:LYS253 4.5 4.9 1.0
CG2 D:THR238 4.6 6.6 1.0
C D:LEU261 4.7 6.3 1.0
CA D:LEU261 4.8 6.3 1.0
C D:GLY262 4.8 7.0 1.0
SG D:CYS263 4.8 6.2 1.0
SG D:CYS242 4.9 5.4 1.0
N D:CYS260 4.9 5.9 1.0
CE D:LYS253 5.0 4.9 1.0

Iron binding site 6 out of 20 in 7uur

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Iron binding site 6 out of 20 in the The 1.67 Angstrom Cryoem Structure of the [Nife]-Hydrogenase Huc From Mycobacterium Smegmatis - Catalytic Dimer (HUC2S2L)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of The 1.67 Angstrom Cryoem Structure of the [Nife]-Hydrogenase Huc From Mycobacterium Smegmatis - Catalytic Dimer (HUC2S2L) within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe403

b:8.8
occ:1.00
FE3 D:F3S403 0.0 8.8 1.0
S1 D:F3S403 2.2 8.8 1.0
S4 D:F3S403 2.3 8.8 1.0
SG D:CYS242 2.3 5.4 1.0
S3 D:F3S403 2.3 8.8 1.0
FE4 D:F3S403 2.6 8.8 1.0
FE1 D:F3S403 2.7 8.8 1.0
CB D:CYS242 3.1 5.4 1.0
O C:HOH810 3.7 6.5 1.0
S2 D:F3S403 4.0 8.8 1.0
OG1 D:THR199 4.0 5.6 1.0
OG D:SER240 4.1 6.1 1.0
NE1 D:TRP247 4.2 6.1 1.0
NZ D:LYS253 4.4 4.9 1.0
CB D:SER240 4.5 6.1 1.0
CG2 D:THR199 4.5 5.6 1.0
CA D:CYS242 4.5 5.4 1.0
SG D:CYS263 4.7 6.2 1.0
OE1 C:GLN163 4.7 5.5 1.0
CH2 D:TRP167 4.7 6.3 1.0
SG D:CYS260 4.7 5.9 1.0
CB D:THR199 4.9 5.6 1.0

Iron binding site 7 out of 20 in 7uur

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Iron binding site 7 out of 20 in the The 1.67 Angstrom Cryoem Structure of the [Nife]-Hydrogenase Huc From Mycobacterium Smegmatis - Catalytic Dimer (HUC2S2L)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of The 1.67 Angstrom Cryoem Structure of the [Nife]-Hydrogenase Huc From Mycobacterium Smegmatis - Catalytic Dimer (HUC2S2L) within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe403

b:8.8
occ:1.00
FE4 D:F3S403 0.0 8.8 1.0
S4 D:F3S403 2.3 8.8 1.0
S2 D:F3S403 2.3 8.8 1.0
SG D:CYS263 2.3 6.2 1.0
S3 D:F3S403 2.3 8.8 1.0
FE3 D:F3S403 2.6 8.8 1.0
FE1 D:F3S403 2.7 8.8 1.0
CB D:CYS263 3.3 6.2 1.0
N D:CYS263 3.6 6.2 1.0
NZ D:LYS253 3.6 4.9 1.0
S1 D:F3S403 3.8 8.8 1.0
CA D:CYS263 3.8 6.2 1.0
N D:THR264 4.1 6.8 1.0
O D:HOH528 4.2 7.4 1.0
O D:HOH516 4.2 6.0 1.0
C D:CYS263 4.3 6.2 1.0
CG2 D:THR264 4.5 6.8 1.0
SG D:CYS242 4.5 5.4 1.0
CE D:LYS253 4.7 4.9 1.0
C D:GLY262 4.7 7.0 1.0
SG D:CYS260 4.7 5.9 1.0
N D:GLY262 4.9 7.0 1.0
CD D:LYS253 5.0 4.9 1.0

Iron binding site 8 out of 20 in 7uur

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Iron binding site 8 out of 20 in the The 1.67 Angstrom Cryoem Structure of the [Nife]-Hydrogenase Huc From Mycobacterium Smegmatis - Catalytic Dimer (HUC2S2L)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of The 1.67 Angstrom Cryoem Structure of the [Nife]-Hydrogenase Huc From Mycobacterium Smegmatis - Catalytic Dimer (HUC2S2L) within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe404

b:11.4
occ:1.00
FE1 D:F3S404 0.0 11.4 1.0
S1 D:F3S404 2.2 11.4 1.0
S2 D:F3S404 2.3 11.4 1.0
SG D:CYS226 2.3 7.5 1.0
S3 D:F3S404 2.3 11.4 1.0
FE3 D:F3S404 2.6 11.4 1.0
FE4 D:F3S404 2.6 11.4 1.0
CB D:CYS226 3.4 7.5 1.0
N D:LEU227 3.8 7.3 1.0
S4 D:F3S404 3.9 11.4 1.0
CA D:CYS226 4.0 7.5 1.0
NE2 D:GLN200 4.1 6.2 1.0
N D:PHE228 4.1 8.9 1.0
CB D:PHE209 4.2 7.8 1.0
C D:CYS226 4.3 7.5 1.0
CD1 D:PHE209 4.3 7.8 1.0
CB D:ARG205 4.4 6.0 1.0
CB D:PHE228 4.4 8.9 1.0
O D:ARG205 4.6 6.0 1.0
CG D:PHE209 4.6 7.8 1.0
CA D:LEU227 4.7 7.3 1.0
SG D:CYS233 4.7 6.5 1.0
CA D:PHE228 4.7 8.9 1.0
SG D:CYS203 4.8 5.8 1.0
C D:ARG205 4.8 6.0 1.0
C D:LEU227 4.8 7.3 1.0
CB D:CYS233 4.9 6.5 1.0

Iron binding site 9 out of 20 in 7uur

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Iron binding site 9 out of 20 in the The 1.67 Angstrom Cryoem Structure of the [Nife]-Hydrogenase Huc From Mycobacterium Smegmatis - Catalytic Dimer (HUC2S2L)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of The 1.67 Angstrom Cryoem Structure of the [Nife]-Hydrogenase Huc From Mycobacterium Smegmatis - Catalytic Dimer (HUC2S2L) within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe404

b:11.4
occ:1.00
FE3 D:F3S404 0.0 11.4 1.0
S1 D:F3S404 2.2 11.4 1.0
S4 D:F3S404 2.3 11.4 1.0
S3 D:F3S404 2.3 11.4 1.0
SG D:CYS233 2.3 6.5 1.0
FE1 D:F3S404 2.6 11.4 1.0
FE4 D:F3S404 2.7 11.4 1.0
CB D:CYS233 3.2 6.5 1.0
S2 D:F3S404 3.9 11.4 1.0
CA D:GLY235 4.1 6.8 1.0
CG2 D:THR254 4.1 5.0 1.0
N D:GLY235 4.2 6.8 1.0
CD D:PRO236 4.4 7.5 1.0
CB D:THR254 4.4 5.0 1.0
CA D:CYS233 4.5 6.5 1.0
SG D:CYS226 4.6 7.5 1.0
CB D:LEU227 4.6 7.3 1.0
N D:PHE228 4.7 8.9 1.0
N D:LEU227 4.7 7.3 1.0
SG D:CYS203 4.7 5.8 1.0
C D:CYS233 4.8 6.5 1.0
C D:LEU227 5.0 7.3 1.0

Iron binding site 10 out of 20 in 7uur

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Iron binding site 10 out of 20 in the The 1.67 Angstrom Cryoem Structure of the [Nife]-Hydrogenase Huc From Mycobacterium Smegmatis - Catalytic Dimer (HUC2S2L)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of The 1.67 Angstrom Cryoem Structure of the [Nife]-Hydrogenase Huc From Mycobacterium Smegmatis - Catalytic Dimer (HUC2S2L) within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe404

b:11.4
occ:1.00
FE4 D:F3S404 0.0 11.4 1.0
S4 D:F3S404 2.3 11.4 1.0
S2 D:F3S404 2.3 11.4 1.0
SG D:CYS203 2.3 5.8 1.0
S3 D:F3S404 2.3 11.4 1.0
FE1 D:F3S404 2.6 11.4 1.0
FE3 D:F3S404 2.7 11.4 1.0
CB D:CYS203 3.0 5.8 1.0
S1 D:F3S404 3.9 11.4 1.0
CB D:THR254 4.0 5.0 1.0
OG1 D:THR254 4.0 5.0 1.0
CB D:ARG205 4.0 6.0 1.0
CA D:CYS203 4.5 5.8 1.0
CG D:GLN200 4.5 6.2 1.0
CG2 D:THR254 4.5 5.0 1.0
N D:ARG205 4.6 6.0 1.0
CD D:ARG205 4.6 6.0 1.0
CA D:ARG205 4.6 6.0 1.0
C D:ARG205 4.6 6.0 1.0
CG D:ARG205 4.7 6.0 1.0
N D:VAL206 4.7 6.5 1.0
CA D:GLN200 4.7 6.2 1.0
SG D:CYS233 4.8 6.5 1.0
NE2 D:GLN200 4.8 6.2 1.0
SG D:CYS226 4.9 7.5 1.0
CG2 D:VAL206 4.9 6.5 1.0
C D:CYS203 4.9 5.8 1.0
CB D:GLN200 4.9 6.2 1.0

Reference:

R.Grinter, A.Kropp, H.Venugopal, M.Senger, J.Badley, P.Cabotaje, S.T.Stripp, C.K.Barlow, M.Belousoff, G.M.Cook, R.B.Schittenhelm, S.Khalid, G.Berggren, G.Greening. An Oxygen-Insensitive, Quinone-Transporting Hydrogenase Enables Bacteria to Extract Energy From Air To Be Published.
Page generated: Fri Aug 9 03:09:54 2024

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