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Iron in PDB 1xk0: Crystal Structures of the G139A, G139A-No and G143H Mutants of Human Heme Oxygenase-1

Enzymatic activity of Crystal Structures of the G139A, G139A-No and G143H Mutants of Human Heme Oxygenase-1

All present enzymatic activity of Crystal Structures of the G139A, G139A-No and G143H Mutants of Human Heme Oxygenase-1:
1.14.99.3;

Protein crystallography data

The structure of Crystal Structures of the G139A, G139A-No and G143H Mutants of Human Heme Oxygenase-1, PDB code: 1xk0 was solved by L.Lad, A.Koshkin, 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 / 2.18
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 54.060, 75.968, 105.299, 90.00, 90.00, 90.00
R / Rfree (%) 22.4 / 26.6

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structures of the G139A, G139A-No and G143H Mutants of Human Heme Oxygenase-1 (pdb code 1xk0). 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 G139A, G139A-No and G143H Mutants of Human Heme Oxygenase-1, PDB code: 1xk0:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 1xk0

Go back to Iron Binding Sites List in 1xk0
Iron binding site 1 out of 2 in the Crystal Structures of the G139A, G139A-No and G143H Mutants of Human Heme Oxygenase-1


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 G139A, G139A-No and G143H Mutants of Human Heme Oxygenase-1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe300

b:53.0
occ:1.00
FE A:HEM300 0.0 53.0 1.0
NA A:HEM300 2.0 53.4 1.0
N A:NO400 2.0 53.2 1.0
NC A:HEM300 2.0 52.8 1.0
ND A:HEM300 2.0 52.8 1.0
NB A:HEM300 2.0 53.4 1.0
NE2 A:HIS25 2.1 54.2 1.0
O A:NO400 3.0 53.8 1.0
CE1 A:HIS25 3.0 55.3 1.0
C1A A:HEM300 3.0 53.7 1.0
C4A A:HEM300 3.0 53.7 1.0
C1D A:HEM300 3.0 52.1 1.0
C4C A:HEM300 3.0 52.4 1.0
C4D A:HEM300 3.1 52.6 1.0
C1C A:HEM300 3.1 52.6 1.0
C1B A:HEM300 3.1 53.4 1.0
C4B A:HEM300 3.1 53.2 1.0
CD2 A:HIS25 3.2 55.5 1.0
CHD A:HEM300 3.4 52.3 1.0
CHA A:HEM300 3.4 53.1 1.0
CHB A:HEM300 3.4 53.7 1.0
CHC A:HEM300 3.5 52.9 1.0
ND1 A:HIS25 4.1 55.7 1.0
CG A:HIS25 4.2 55.5 1.0
C2A A:HEM300 4.2 54.3 1.0
C3A A:HEM300 4.2 54.1 1.0
C2D A:HEM300 4.3 52.0 1.0
C3C A:HEM300 4.3 52.5 1.0
C3D A:HEM300 4.3 52.1 1.0
C2C A:HEM300 4.3 52.5 1.0
C2B A:HEM300 4.3 53.7 1.0
C3B A:HEM300 4.4 53.6 1.0

Iron binding site 2 out of 2 in 1xk0

Go back to Iron Binding Sites List in 1xk0
Iron binding site 2 out of 2 in the Crystal Structures of the G139A, G139A-No and G143H Mutants of Human Heme Oxygenase-1


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 G139A, G139A-No and G143H Mutants of Human Heme Oxygenase-1 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe300

b:53.4
occ:1.00
FE B:HEM300 0.0 53.4 1.0
NB B:HEM300 2.0 53.7 1.0
ND B:HEM300 2.0 53.4 1.0
NC B:HEM300 2.0 53.0 1.0
NA B:HEM300 2.0 54.3 1.0
NE2 B:HIS25 2.1 53.5 1.0
CE1 B:HIS25 3.0 53.1 1.0
C1D B:HEM300 3.0 53.1 1.0
C4D B:HEM300 3.0 53.6 1.0
C4B B:HEM300 3.0 53.6 1.0
C1B B:HEM300 3.0 53.8 1.0
C4C B:HEM300 3.0 52.8 1.0
C1C B:HEM300 3.1 52.9 1.0
C4A B:HEM300 3.1 54.5 1.0
C1A B:HEM300 3.1 54.6 1.0
CD2 B:HIS25 3.1 53.0 1.0
CHD B:HEM300 3.4 52.8 1.0
CHC B:HEM300 3.4 53.0 1.0
CHA B:HEM300 3.4 54.1 1.0
CHB B:HEM300 3.5 54.1 1.0
ND1 B:HIS25 4.1 53.1 1.0
CG B:HIS25 4.2 52.7 1.0
C2D B:HEM300 4.3 53.3 1.0
C3D B:HEM300 4.3 53.6 1.0
C3B B:HEM300 4.3 53.9 1.0
C2B B:HEM300 4.3 53.8 1.0
C3A B:HEM300 4.3 55.1 1.0
C3C B:HEM300 4.3 52.7 1.0
C2C B:HEM300 4.3 52.6 1.0
C2A B:HEM300 4.3 55.3 1.0
O B:HOH359 4.9 44.6 1.0

Reference:

L.Lad, A.Koshkin, P.R.Ortiz De Montellano, T.L.Poulos. Crystal Structures of the G139A, G139A-No and G143H Mutants of Human Heme Oxygenase-1. A Finely Tuned Hydrogen-Bonding Network Controls Oxygenase Versus Peroxidase Activity. J.Biol.Inorg.Chem. V. 10 138 2005.
ISSN: ISSN 0949-8257
PubMed: 15690204
DOI: 10.1007/S00775-004-0620-6
Page generated: Sun Dec 13 14:35:52 2020

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