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Iron in PDB 1oyl: 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: 1oyl 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 / 1.59
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 61.587, 54.696, 71.138, 90.00, 99.57, 90.00
R / Rfree (%) 22.4 / 24.3

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

Iron binding site 1 out of 2 in 1oyl

Go back to Iron Binding Sites List in 1oyl
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:31.1
occ:1.00
 FE A:HEM300 0.0 31.1 1.0
O A:HOH455 1.9 31.2 1.0
NA A:HEM300 2.0 31.5 1.0
ND A:HEM300 2.0 31.1 1.0
NC A:HEM300 2.0 31.1 1.0
NB A:HEM300 2.0 31.4 1.0
NE2 A:HIS25 2.1 31.1 1.0
C1A A:HEM300 3.0 31.5 1.0
C4D A:HEM300 3.0 31.2 1.0
C1D A:HEM300 3.0 31.0 1.0
C4A A:HEM300 3.1 31.6 1.0
C4C A:HEM300 3.1 31.1 1.0
C1B A:HEM300 3.1 31.6 1.0
C4B A:HEM300 3.1 31.5 1.0
C1C A:HEM300 3.1 31.2 1.0
CE1 A:HIS25 3.1 31.0 1.0
CD2 A:HIS25 3.1 30.9 1.0
CHA A:HEM300 3.4 31.4 1.0
CHD A:HEM300 3.4 31.0 1.0
CHB A:HEM300 3.5 31.6 1.0
CHC A:HEM300 3.5 31.4 1.0
ND1 A:HIS25 4.2 31.0 1.0
CG A:HIS25 4.2 31.0 1.0
C3D A:HEM300 4.3 31.2 1.0
C2D A:HEM300 4.3 31.0 1.0
C2A A:HEM300 4.3 31.8 1.0
C3A A:HEM300 4.3 31.8 1.0
C2B A:HEM300 4.3 31.7 1.0
C3C A:HEM300 4.3 31.2 1.0
C3B A:HEM300 4.3 31.7 1.0
C2C A:HEM300 4.3 31.2 1.0
O A:HOH517 4.5 48.0 1.0
O A:GLY139 4.8 29.7 1.0

Iron binding site 2 out of 2 in 1oyl

Go back to Iron Binding Sites List in 1oyl
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:35.4
occ:1.00
 FE B:HEM300 0.0 35.4 1.0
ND B:HEM300 2.0 35.4 1.0
NA B:HEM300 2.0 35.6 1.0
NB B:HEM300 2.0 35.6 1.0
NC B:HEM300 2.0 35.4 1.0
NE2 B:HIS25 2.1 35.8 1.0
O B:HOH457 2.2 35.5 1.0
CE1 B:HIS25 3.0 36.3 1.0
C1D B:HEM300 3.0 35.3 1.0
C4A B:HEM300 3.0 35.7 1.0
C1B B:HEM300 3.0 35.7 1.0
C4D B:HEM300 3.0 35.3 1.0
C1A B:HEM300 3.0 35.6 1.0
C4C B:HEM300 3.0 35.3 1.0
C4B B:HEM300 3.1 35.6 1.0
C1C B:HEM300 3.1 35.4 1.0
CD2 B:HIS25 3.1 36.4 1.0
CHA B:HEM300 3.4 35.5 1.0
CHB B:HEM300 3.4 35.8 1.0
CHD B:HEM300 3.4 35.2 1.0
CHC B:HEM300 3.4 35.5 1.0
ND1 B:HIS25 4.2 36.4 1.0
CG B:HIS25 4.2 36.7 1.0
C2D B:HEM300 4.3 35.3 1.0
C3D B:HEM300 4.3 35.3 1.0
C3A B:HEM300 4.3 35.8 1.0
C2B B:HEM300 4.3 35.8 1.0
C2A B:HEM300 4.3 35.9 1.0
C3C B:HEM300 4.3 35.4 1.0
C2C B:HEM300 4.3 35.4 1.0
C3B B:HEM300 4.3 35.7 1.0
O B:SER142 4.4 35.1 0.6
O B:GLY139 4.9 29.3 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 12:44:40 2024

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