Atomistry » Iron » PDB 1ofj-1ozl » 1oze
Atomistry »
  Iron »
    PDB 1ofj-1ozl »
      1oze »

Iron in PDB 1oze: 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: 1oze 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 / 2.19
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 61.662, 54.368, 71.748, 90.00, 99.82, 90.00
R / Rfree (%) 20.9 / 26

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 1oze). 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: 1oze:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 1oze

Go back to Iron Binding Sites List in 1oze
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:38.2
occ:1.00
 FE A:HEM300 0.0 38.2 1.0
NA A:HEM300 2.0 40.0 1.0
NC A:HEM300 2.0 38.6 1.0
ND A:HEM300 2.0 38.0 1.0
NB A:HEM300 2.0 39.6 1.0
NE2 A:HIS25 2.1 37.0 1.0
C1A A:HEM300 3.0 40.5 1.0
C4A A:HEM300 3.0 40.8 1.0
C4C A:HEM300 3.0 38.7 1.0
C4D A:HEM300 3.0 38.0 1.0
C1D A:HEM300 3.1 37.2 1.0
C1C A:HEM300 3.1 39.1 1.0
C4B A:HEM300 3.1 39.7 1.0
C1B A:HEM300 3.1 40.0 1.0
CE1 A:HIS25 3.1 35.5 1.0
CD2 A:HIS25 3.1 35.7 1.0
CHA A:HEM300 3.4 39.6 1.0
CHD A:HEM300 3.4 37.5 1.0
CHC A:HEM300 3.4 39.8 1.0
CHB A:HEM300 3.4 39.8 1.0
O A:HOH353 3.8 52.4 1.0
ND1 A:HIS25 4.2 36.0 1.0
CG A:HIS25 4.3 36.7 1.0
C3A A:HEM300 4.3 41.2 1.0
C2A A:HEM300 4.3 41.8 1.0
C3C A:HEM300 4.3 39.2 1.0
C2B A:HEM300 4.3 40.3 1.0
C2D A:HEM300 4.3 37.8 1.0
C2C A:HEM300 4.3 39.4 1.0
C3B A:HEM300 4.3 41.2 1.0
C3D A:HEM300 4.3 38.1 1.0
O A:HOH357 4.7 48.1 1.0
O A:GLY139 4.8 34.9 1.0
CA A:GLY143 4.9 47.3 1.0
CA A:GLY139 4.9 33.5 1.0
N A:GLY143 4.9 45.8 1.0

Iron binding site 2 out of 2 in 1oze

Go back to Iron Binding Sites List in 1oze
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:59.3
occ:1.00
 FE B:HEM300 0.0 59.3 1.0
NA B:HEM300 2.0 61.0 1.0
NB B:HEM300 2.0 60.5 1.0
ND B:HEM300 2.0 59.1 1.0
NC B:HEM300 2.0 58.9 1.0
NE2 B:HIS25 2.1 56.6 1.0
CE1 B:HIS25 3.0 53.6 1.0
C1A B:HEM300 3.0 61.7 1.0
C4A B:HEM300 3.0 62.2 1.0
C4D B:HEM300 3.0 59.8 1.0
C1B B:HEM300 3.1 61.4 1.0
C4B B:HEM300 3.1 60.9 1.0
C1D B:HEM300 3.1 58.9 1.0
C1C B:HEM300 3.1 59.3 1.0
C4C B:HEM300 3.1 58.5 1.0
CD2 B:HIS25 3.2 53.6 1.0
CHA B:HEM300 3.4 60.5 1.0
CHB B:HEM300 3.4 61.7 1.0
CHC B:HEM300 3.4 59.9 1.0
CHD B:HEM300 3.5 58.4 1.0
ND1 B:HIS25 4.1 53.4 1.0
CG B:HIS25 4.2 53.2 1.0
C2A B:HEM300 4.3 63.5 1.0
C3D B:HEM300 4.3 59.8 1.0
C3A B:HEM300 4.3 63.3 1.0
C2B B:HEM300 4.3 62.0 1.0
C2D B:HEM300 4.3 58.7 1.0
C3B B:HEM300 4.3 61.9 1.0
C2C B:HEM300 4.3 59.2 1.0
C3C B:HEM300 4.3 59.1 1.0
O B:GLY139 5.0 37.8 1.0
CA B:GLY139 5.0 36.1 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: Sat Aug 3 12:45:17 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy