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Iron in PDB 2isa: Crystal Structure of Vibrio Salmonicida Catalase

Enzymatic activity of Crystal Structure of Vibrio Salmonicida Catalase

All present enzymatic activity of Crystal Structure of Vibrio Salmonicida Catalase:
1.11.1.6;

Protein crystallography data

The structure of Crystal Structure of Vibrio Salmonicida Catalase, PDB code: 2isa was solved by E.K.Riise, M.S.Lorentzen, R.Helland, A.O.Smalas, H.K.S.Leiros, N.P.Willassen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.97
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 98.150, 217.760, 99.280, 90.00, 110.48, 90.00
R / Rfree (%) 14.8 / 20

Other elements in 2isa:

The structure of Crystal Structure of Vibrio Salmonicida Catalase also contains other interesting chemical elements:

Chlorine (Cl) 4 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Vibrio Salmonicida Catalase (pdb code 2isa). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 8 binding sites of Iron where determined in the Crystal Structure of Vibrio Salmonicida Catalase, PDB code: 2isa:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Iron binding site 1 out of 8 in 2isa

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Iron binding site 1 out of 8 in the Crystal Structure of Vibrio Salmonicida Catalase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of Vibrio Salmonicida Catalase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe486

b:8.9
occ:1.00
FE A:HEM486 0.0 8.9 1.0
OH A:TYR337 2.0 7.5 1.0
NC A:HEM486 2.0 8.4 1.0
NA A:HEM486 2.1 7.9 1.0
ND A:HEM486 2.1 7.4 1.0
NB A:HEM486 2.1 7.9 1.0
C1A A:HEM486 3.0 8.3 1.0
C4C A:HEM486 3.0 8.2 1.0
CZ A:TYR337 3.0 6.3 1.0
C1C A:HEM486 3.1 7.9 1.0
C1D A:HEM486 3.1 7.4 1.0
C4D A:HEM486 3.1 9.4 1.0
C4B A:HEM486 3.1 8.8 1.0
C4A A:HEM486 3.1 7.5 1.0
C1B A:HEM486 3.1 7.9 1.0
CHA A:HEM486 3.4 8.4 1.0
CHD A:HEM486 3.4 7.3 1.0
CHC A:HEM486 3.4 9.1 1.0
CHB A:HEM486 3.5 8.3 1.0
CE2 A:TYR337 3.8 5.5 1.0
O A:HOH5671 3.8 22.8 1.0
CE1 A:TYR337 3.9 5.0 1.0
NE A:ARG333 4.1 5.9 1.0
NH2 A:ARG333 4.2 3.6 1.0
C3C A:HEM486 4.3 8.4 1.0
C2A A:HEM486 4.3 6.4 1.0
C2C A:HEM486 4.3 10.0 1.0
C2D A:HEM486 4.3 8.4 1.0
C3A A:HEM486 4.3 9.2 1.0
C3D A:HEM486 4.3 7.6 1.0
C3B A:HEM486 4.3 8.6 1.0
C2B A:HEM486 4.3 8.5 1.0
CZ A:PHE140 4.5 9.6 1.0
CZ A:ARG333 4.6 6.1 1.0
NE2 A:HIS54 4.7 6.3 1.0
CD2 A:HIS54 4.7 7.2 1.0
CE1 A:PHE140 4.9 9.1 1.0

Iron binding site 2 out of 8 in 2isa

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Iron binding site 2 out of 8 in the Crystal Structure of Vibrio Salmonicida Catalase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of Vibrio Salmonicida Catalase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe486

b:10.8
occ:1.00
FE B:HEM486 0.0 10.8 1.0
OH B:TYR337 1.8 6.3 1.0
NB B:HEM486 2.1 8.7 1.0
ND B:HEM486 2.1 7.8 1.0
NA B:HEM486 2.1 8.3 1.0
NC B:HEM486 2.1 8.0 1.0
CZ B:TYR337 2.9 7.8 1.0
C4D B:HEM486 3.1 7.1 1.0
C4C B:HEM486 3.1 8.0 1.0
C1D B:HEM486 3.1 8.2 1.0
C1B B:HEM486 3.1 9.0 1.0
C1A B:HEM486 3.1 8.1 1.0
C4B B:HEM486 3.1 8.3 1.0
C4A B:HEM486 3.1 7.6 1.0
C1C B:HEM486 3.1 8.4 1.0
CHA B:HEM486 3.4 7.1 1.0
CHD B:HEM486 3.4 6.9 1.0
CHB B:HEM486 3.5 7.6 1.0
CHC B:HEM486 3.5 7.4 1.0
CE2 B:TYR337 3.7 8.4 1.0
CE1 B:TYR337 3.8 8.1 1.0
O B:HOH6594 4.1 18.1 1.0
NH2 B:ARG333 4.1 6.0 1.0
NE B:ARG333 4.2 7.0 1.0
C2B B:HEM486 4.3 8.5 1.0
C3B B:HEM486 4.3 8.0 1.0
C3D B:HEM486 4.3 6.9 1.0
C3C B:HEM486 4.3 7.0 1.0
C2D B:HEM486 4.3 6.7 1.0
C2A B:HEM486 4.3 8.2 1.0
C2C B:HEM486 4.3 7.7 1.0
C3A B:HEM486 4.3 8.2 1.0
CZ B:PHE140 4.4 8.7 1.0
NE2 B:HIS54 4.6 6.1 1.0
CZ B:ARG333 4.6 7.2 1.0
CD2 B:HIS54 4.7 7.1 1.0
CE1 B:PHE140 4.8 10.1 1.0
CD2 B:TYR337 5.0 7.1 1.0

Iron binding site 3 out of 8 in 2isa

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Iron binding site 3 out of 8 in the Crystal Structure of Vibrio Salmonicida Catalase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Crystal Structure of Vibrio Salmonicida Catalase within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe485

b:10.2
occ:1.00
FE C:HEM485 0.0 10.2 1.0
OH C:TYR337 1.8 7.5 1.0
NC C:HEM485 2.0 7.9 1.0
NA C:HEM485 2.1 7.9 1.0
NB C:HEM485 2.1 8.8 1.0
ND C:HEM485 2.1 6.0 1.0
CZ C:TYR337 3.0 7.6 1.0
C1A C:HEM485 3.0 7.2 1.0
C4C C:HEM485 3.1 7.0 1.0
C1C C:HEM485 3.1 9.0 1.0
C4B C:HEM485 3.1 8.9 1.0
C4D C:HEM485 3.1 6.7 1.0
C4A C:HEM485 3.1 8.2 1.0
C1B C:HEM485 3.1 9.7 1.0
C1D C:HEM485 3.1 6.0 1.0
CHA C:HEM485 3.4 6.1 1.0
CHC C:HEM485 3.4 8.2 1.0
CHD C:HEM485 3.5 6.8 1.0
CHB C:HEM485 3.5 7.8 1.0
CE2 C:TYR337 3.8 7.8 1.0
CE1 C:TYR337 3.9 6.9 1.0
O C:HOH5626 4.1 25.3 1.0
NH2 C:ARG333 4.2 8.9 1.0
NE C:ARG333 4.2 7.5 1.0
C2A C:HEM485 4.3 7.1 1.0
C3C C:HEM485 4.3 7.7 1.0
C2C C:HEM485 4.3 7.3 1.0
C3A C:HEM485 4.3 7.6 1.0
C3B C:HEM485 4.3 9.4 1.0
C2B C:HEM485 4.3 9.5 1.0
C3D C:HEM485 4.3 4.9 1.0
CZ C:PHE140 4.3 7.0 1.0
C2D C:HEM485 4.4 5.4 1.0
CZ C:ARG333 4.6 10.2 1.0
NE2 C:HIS54 4.6 2.0 1.0
CD2 C:HIS54 4.7 4.0 1.0
CE1 C:PHE140 4.8 7.6 1.0

Iron binding site 4 out of 8 in 2isa

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Iron binding site 4 out of 8 in the Crystal Structure of Vibrio Salmonicida Catalase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Crystal Structure of Vibrio Salmonicida Catalase within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe485

b:12.3
occ:1.00
FE D:HEM485 0.0 12.3 1.0
OH D:TYR337 1.9 7.8 1.0
NB D:HEM485 2.1 11.8 1.0
NC D:HEM485 2.1 10.5 1.0
NA D:HEM485 2.1 10.9 1.0
ND D:HEM485 2.1 10.5 1.0
CZ D:TYR337 3.0 7.7 1.0
C1B D:HEM485 3.0 11.6 1.0
C4C D:HEM485 3.1 10.2 1.0
C4B D:HEM485 3.1 11.9 1.0
C4A D:HEM485 3.1 10.9 1.0
C1C D:HEM485 3.1 10.5 1.0
C1D D:HEM485 3.1 10.7 1.0
C1A D:HEM485 3.1 9.8 1.0
C4D D:HEM485 3.1 11.6 1.0
CHB D:HEM485 3.4 10.4 1.0
CHD D:HEM485 3.4 10.1 1.0
CHC D:HEM485 3.5 10.9 1.0
CHA D:HEM485 3.5 10.4 1.0
CE2 D:TYR337 3.8 8.1 1.0
CE1 D:TYR337 3.9 8.4 1.0
NE D:ARG333 4.1 6.3 1.0
NH2 D:ARG333 4.2 7.2 1.0
C2B D:HEM485 4.2 11.3 1.0
O D:HOH5669 4.2 24.8 1.0
C3B D:HEM485 4.3 11.0 1.0
C3C D:HEM485 4.3 10.3 1.0
C2C D:HEM485 4.3 10.3 1.0
C3A D:HEM485 4.3 9.4 1.0
C2A D:HEM485 4.3 9.3 1.0
CZ D:PHE140 4.3 10.9 1.0
C2D D:HEM485 4.3 10.5 1.0
C3D D:HEM485 4.4 9.6 1.0
CZ D:ARG333 4.6 7.0 1.0
NE2 D:HIS54 4.6 7.9 1.0
CD2 D:HIS54 4.7 8.7 1.0
CE1 D:PHE140 4.8 11.2 1.0

Iron binding site 5 out of 8 in 2isa

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Iron binding site 5 out of 8 in the Crystal Structure of Vibrio Salmonicida Catalase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Crystal Structure of Vibrio Salmonicida Catalase within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Fe486

b:12.7
occ:1.00
FE E:HEM486 0.0 12.7 1.0
OH E:TYR337 1.8 10.7 1.0
NA E:HEM486 2.1 10.2 1.0
ND E:HEM486 2.1 10.9 1.0
NC E:HEM486 2.1 11.6 1.0
NB E:HEM486 2.1 12.0 1.0
CZ E:TYR337 2.9 10.2 1.0
C1A E:HEM486 3.0 10.5 1.0
C4D E:HEM486 3.0 10.4 1.0
C4C E:HEM486 3.1 11.3 1.0
C1D E:HEM486 3.1 10.7 1.0
C4A E:HEM486 3.1 10.0 1.0
C1B E:HEM486 3.1 11.3 1.0
C4B E:HEM486 3.1 11.6 1.0
C1C E:HEM486 3.1 12.0 1.0
O E:HOH5919 3.2 34.2 1.0
CHA E:HEM486 3.4 9.6 1.0
CHD E:HEM486 3.4 10.3 1.0
CHC E:HEM486 3.5 11.8 1.0
CHB E:HEM486 3.5 10.8 1.0
CE2 E:TYR337 3.6 10.8 1.0
CE1 E:TYR337 3.9 11.1 1.0
NE E:ARG333 4.1 9.8 1.0
NH2 E:ARG333 4.1 9.4 1.0
C2A E:HEM486 4.3 10.8 1.0
C3D E:HEM486 4.3 10.1 1.0
C3C E:HEM486 4.3 11.6 1.0
C3A E:HEM486 4.3 11.6 1.0
C3B E:HEM486 4.3 11.5 1.0
C2B E:HEM486 4.3 12.0 1.0
C2C E:HEM486 4.3 11.7 1.0
C2D E:HEM486 4.3 8.9 1.0
CZ E:PHE140 4.4 11.8 1.0
O E:HOH5718 4.5 21.9 1.0
CZ E:ARG333 4.5 10.6 1.0
CD2 E:HIS54 4.7 11.1 1.0
NE2 E:HIS54 4.7 11.0 1.0
CE1 E:PHE140 4.8 13.4 1.0
CD2 E:TYR337 4.9 9.6 1.0

Iron binding site 6 out of 8 in 2isa

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Iron binding site 6 out of 8 in the Crystal Structure of Vibrio Salmonicida Catalase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Crystal Structure of Vibrio Salmonicida Catalase within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Fe486

b:12.6
occ:1.00
FE F:HEM486 0.0 12.6 1.0
OH F:TYR337 1.8 10.7 1.0
ND F:HEM486 2.0 10.8 1.0
NA F:HEM486 2.1 11.5 1.0
NC F:HEM486 2.1 11.4 1.0
NB F:HEM486 2.1 11.8 1.0
CZ F:TYR337 3.0 10.2 1.0
C1D F:HEM486 3.0 11.4 1.0
C4D F:HEM486 3.0 11.5 1.0
C4C F:HEM486 3.1 11.5 1.0
C4A F:HEM486 3.1 12.7 1.0
C1A F:HEM486 3.1 11.0 1.0
C1B F:HEM486 3.1 13.2 1.0
C4B F:HEM486 3.2 12.7 1.0
C1C F:HEM486 3.2 11.6 1.0
CHD F:HEM486 3.4 11.3 1.0
CHB F:HEM486 3.4 12.2 1.0
CHA F:HEM486 3.4 11.2 1.0
CHC F:HEM486 3.6 12.1 1.0
CE2 F:TYR337 3.8 11.2 1.0
CE1 F:TYR337 3.8 10.1 1.0
O F:HOH8597 4.0 28.4 1.0
NE F:ARG333 4.2 9.3 1.0
C2D F:HEM486 4.2 9.8 1.0
C3D F:HEM486 4.3 10.1 1.0
NH2 F:ARG333 4.3 10.9 1.0
C2A F:HEM486 4.3 12.5 1.0
C3A F:HEM486 4.3 13.1 1.0
C3C F:HEM486 4.3 11.2 1.0
C2B F:HEM486 4.3 13.5 1.0
C3B F:HEM486 4.3 12.7 1.0
C2C F:HEM486 4.4 12.3 1.0
CZ F:PHE140 4.4 11.6 1.0
NE2 F:HIS54 4.7 9.3 1.0
CZ F:ARG333 4.7 11.6 1.0
CD2 F:HIS54 4.7 10.7 1.0
CE1 F:PHE140 4.8 11.8 1.0

Iron binding site 7 out of 8 in 2isa

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Iron binding site 7 out of 8 in the Crystal Structure of Vibrio Salmonicida Catalase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Crystal Structure of Vibrio Salmonicida Catalase within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Fe485

b:11.6
occ:1.00
FE G:HEM485 0.0 11.6 1.0
OH G:TYR337 1.9 9.6 1.0
NA G:HEM485 2.0 9.9 1.0
ND G:HEM485 2.1 12.2 1.0
NC G:HEM485 2.1 11.8 1.0
NB G:HEM485 2.1 11.4 1.0
CZ G:TYR337 2.9 8.8 1.0
C4C G:HEM485 3.0 12.0 1.0
C1D G:HEM485 3.0 10.9 1.0
C1A G:HEM485 3.1 9.7 1.0
C4A G:HEM485 3.1 11.2 1.0
C4D G:HEM485 3.1 10.6 1.0
C1B G:HEM485 3.1 11.6 1.0
C1C G:HEM485 3.1 11.4 1.0
C4B G:HEM485 3.2 12.4 1.0
CHD G:HEM485 3.4 11.5 1.0
CHA G:HEM485 3.4 10.2 1.0
CHB G:HEM485 3.4 10.9 1.0
CHC G:HEM485 3.5 11.7 1.0
CE2 G:TYR337 3.7 8.2 1.0
CE1 G:TYR337 3.8 7.9 1.0
NE G:ARG333 4.2 8.8 1.0
O G:HOH5654 4.2 19.2 1.0
NH2 G:ARG333 4.2 9.6 1.0
C2A G:HEM485 4.3 9.7 1.0
C3A G:HEM485 4.3 10.1 1.0
C3C G:HEM485 4.3 11.5 1.0
C2D G:HEM485 4.3 11.4 1.0
C3D G:HEM485 4.3 10.4 1.0
C2B G:HEM485 4.3 12.0 1.0
C2C G:HEM485 4.3 11.5 1.0
CZ G:PHE140 4.3 10.5 1.0
C3B G:HEM485 4.4 12.3 1.0
NE2 G:HIS54 4.6 8.2 1.0
CZ G:ARG333 4.6 10.7 1.0
CD2 G:HIS54 4.6 9.2 1.0
CE1 G:PHE140 4.8 12.7 1.0
CD2 G:TYR337 5.0 9.6 1.0

Iron binding site 8 out of 8 in 2isa

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Iron binding site 8 out of 8 in the Crystal Structure of Vibrio Salmonicida Catalase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Crystal Structure of Vibrio Salmonicida Catalase within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Fe485

b:12.6
occ:1.00
FE H:HEM485 0.0 12.6 1.0
OH H:TYR337 1.9 10.0 1.0
NB H:HEM485 2.0 10.5 1.0
NC H:HEM485 2.1 11.7 1.0
NA H:HEM485 2.1 12.2 1.0
ND H:HEM485 2.1 10.5 1.0
CZ H:TYR337 3.0 9.8 1.0
C1B H:HEM485 3.0 11.2 1.0
C4B H:HEM485 3.1 11.2 1.0
C4A H:HEM485 3.1 12.5 1.0
C1C H:HEM485 3.1 11.4 1.0
C4C H:HEM485 3.1 12.1 1.0
C1D H:HEM485 3.1 11.2 1.0
C4D H:HEM485 3.1 10.6 1.0
C1A H:HEM485 3.1 12.2 1.0
O H:HOH7891 3.2 25.7 1.0
CHB H:HEM485 3.4 11.8 1.0
CHC H:HEM485 3.4 9.8 1.0
CHD H:HEM485 3.4 10.2 1.0
CHA H:HEM485 3.5 10.3 1.0
CE2 H:TYR337 3.7 9.5 1.0
CE1 H:TYR337 3.8 10.4 1.0
NE H:ARG333 4.0 10.0 1.0
NH2 H:ARG333 4.1 6.9 1.0
C2B H:HEM485 4.3 10.1 1.0
C3B H:HEM485 4.3 11.0 1.0
C2C H:HEM485 4.3 10.5 1.0
C3C H:HEM485 4.3 12.2 1.0
C3A H:HEM485 4.3 13.2 1.0
C2A H:HEM485 4.3 11.9 1.0
C3D H:HEM485 4.3 9.1 1.0
C2D H:HEM485 4.3 10.5 1.0
CZ H:PHE140 4.4 11.6 1.0
CZ H:ARG333 4.5 10.7 1.0
NE2 H:HIS54 4.6 7.3 1.0
O H:HOH7765 4.6 24.2 1.0
CD2 H:HIS54 4.6 8.5 1.0
CE1 H:PHE140 4.8 13.2 1.0
CD2 H:TYR337 5.0 10.4 1.0

Reference:

E.K.Riise, M.S.Lorentzen, R.Helland, A.O.Smalas, H.K.S.Leiros, N.P.Willassen. The First Structure of A Cold-Active Catalase From Vibrio Salmonicida at 1.96A Reveals Structural Aspects of Cold Adaptation Acta Crystallogr.,Sect.D V. 63 135 2007.
ISSN: ISSN 0907-4449
PubMed: 17242507
DOI: 10.1107/S0907444906043812
Page generated: Thu Jul 17 02:19:13 2025

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