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Iron in PDB 1oyk: Crystal Structures of the Ferric, Ferrous, and Ferrous-No Forms of the ASP140ALA Mutant of Human Heme Oxygenase-1: Catalytic Implications

Enzymatic activity of Crystal Structures of the Ferric, Ferrous, and Ferrous-No Forms of the ASP140ALA Mutant of Human Heme Oxygenase-1: Catalytic Implications

All present enzymatic activity of Crystal Structures of the Ferric, Ferrous, and Ferrous-No Forms of the ASP140ALA Mutant of Human Heme Oxygenase-1: Catalytic Implications:
1.14.99.3;

Protein crystallography data

The structure of Crystal Structures of the Ferric, Ferrous, and Ferrous-No Forms of the ASP140ALA Mutant of Human Heme Oxygenase-1: Catalytic Implications, PDB code: 1oyk was solved by L.Lad, J.Wang, H.Li, J.Friedman, P.R.Ortiz De Montellano, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.59
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 55.665, 77.662, 100.318, 90.00, 90.00, 90.00
R / Rfree (%) 23.4 / 30.9

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structures of the Ferric, Ferrous, and Ferrous-No Forms of the ASP140ALA Mutant of Human Heme Oxygenase-1: Catalytic Implications (pdb code 1oyk). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structures of the Ferric, Ferrous, and Ferrous-No Forms of the ASP140ALA Mutant of Human Heme Oxygenase-1: Catalytic Implications, PDB code: 1oyk:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 1oyk

Go back to Iron Binding Sites List in 1oyk
Iron binding site 1 out of 2 in the Crystal Structures of the Ferric, Ferrous, and Ferrous-No Forms of the ASP140ALA Mutant of Human Heme Oxygenase-1: Catalytic Implications


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structures of the Ferric, Ferrous, and Ferrous-No Forms of the ASP140ALA Mutant of Human Heme Oxygenase-1: Catalytic Implications within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe300

b:70.9
occ:1.00
 FE A:HEM300 0.0 70.9 1.0
NC A:HEM300 2.0 70.7 1.0
NA A:HEM300 2.0 71.3 1.0
NB A:HEM300 2.0 71.0 1.0
ND A:HEM300 2.0 71.0 1.0
NE2 A:HIS25 2.2 71.6 1.0
C4C A:HEM300 3.0 70.5 1.0
C1C A:HEM300 3.0 70.6 1.0
C4A A:HEM300 3.0 71.4 1.0
C1B A:HEM300 3.0 71.0 1.0
C1D A:HEM300 3.1 70.6 1.0
CE1 A:HIS25 3.1 71.9 1.0
C4B A:HEM300 3.1 70.8 1.0
C4D A:HEM300 3.1 71.0 1.0
C1A A:HEM300 3.1 71.5 1.0
CD2 A:HIS25 3.2 72.3 1.0
CHD A:HEM300 3.4 70.5 1.0
CHC A:HEM300 3.4 70.8 1.0
CHB A:HEM300 3.4 71.1 1.0
CHA A:HEM300 3.5 71.3 1.0
ND1 A:HIS25 4.2 72.2 1.0
C2C A:HEM300 4.2 70.5 1.0
C3C A:HEM300 4.3 70.5 1.0
C3A A:HEM300 4.3 71.8 1.0
C2D A:HEM300 4.3 70.7 1.0
C3D A:HEM300 4.3 70.9 1.0
C2B A:HEM300 4.3 71.0 1.0
C3B A:HEM300 4.3 70.9 1.0
C2A A:HEM300 4.3 72.0 1.0
CG A:HIS25 4.3 72.5 1.0
O A:GLY139 4.8 59.8 1.0

Iron binding site 2 out of 2 in 1oyk

Go back to Iron Binding Sites List in 1oyk
Iron binding site 2 out of 2 in the Crystal Structures of the Ferric, Ferrous, and Ferrous-No Forms of the ASP140ALA Mutant of Human Heme Oxygenase-1: Catalytic Implications


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structures of the Ferric, Ferrous, and Ferrous-No Forms of the ASP140ALA Mutant of Human Heme Oxygenase-1: Catalytic Implications within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe300

b:66.8
occ:1.00
 FE B:HEM300 0.0 66.8 1.0
NC B:HEM300 2.0 67.0 1.0
ND B:HEM300 2.0 66.7 1.0
NB B:HEM300 2.0 67.2 1.0
NA B:HEM300 2.0 67.3 1.0
NE2 B:HIS25 2.1 66.8 1.0
CE1 B:HIS25 2.7 66.4 1.0
O B:HOH320 2.9 47.5 1.0
C4C B:HEM300 3.0 66.8 1.0
C1C B:HEM300 3.0 67.0 1.0
C1D B:HEM300 3.0 66.5 1.0
C4D B:HEM300 3.0 66.8 1.0
C4B B:HEM300 3.1 67.2 1.0
C1A B:HEM300 3.1 67.5 1.0
C1B B:HEM300 3.1 67.3 1.0
C4A B:HEM300 3.1 67.4 1.0
CD2 B:HIS25 3.3 66.4 1.0
CHD B:HEM300 3.4 66.7 1.0
CHC B:HEM300 3.4 67.2 1.0
CHA B:HEM300 3.4 67.2 1.0
CHB B:HEM300 3.5 67.2 1.0
ND1 B:HIS25 3.9 66.6 1.0
CG B:HIS25 4.2 66.5 1.0
C3C B:HEM300 4.2 66.8 1.0
C2D B:HEM300 4.3 66.6 1.0
C3D B:HEM300 4.3 66.6 1.0
C2C B:HEM300 4.3 66.9 1.0
C3A B:HEM300 4.3 67.8 1.0
C3B B:HEM300 4.3 67.3 1.0
C2B B:HEM300 4.3 67.4 1.0
C2A B:HEM300 4.3 68.0 1.0
CA B:GLY139 4.8 44.4 1.0
O B:SER142 4.8 60.4 1.0
O B:GLY139 5.0 45.4 1.0

Reference:

L.Lad, J.Wang, H.Li, J.Friedman, B.Bhaskar, P.R.Ortiz De Montellano, T.L.Poulos. Crystal Structures of the Ferric, Ferrous, and Ferrous-No Forms of the ASP140ALA Mutant of Human Heme Oxygenase-1: Catalytic Implications J.Mol.Biol. V. 330 527 2003.
ISSN: ISSN 0022-2836
PubMed: 12842469
DOI: 10.1016/S0022-2836(03)00578-3
Page generated: Wed Jul 16 19:26:19 2025

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