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Iron in PDB 1wzg: Crystal Structure of An Artificial Metalloprotein: Fe(Salophen)/Wild Type Heme Oxygenase

Enzymatic activity of Crystal Structure of An Artificial Metalloprotein: Fe(Salophen)/Wild Type Heme Oxygenase

All present enzymatic activity of Crystal Structure of An Artificial Metalloprotein: Fe(Salophen)/Wild Type Heme Oxygenase:
1.14.99.3;

Protein crystallography data

The structure of Crystal Structure of An Artificial Metalloprotein: Fe(Salophen)/Wild Type Heme Oxygenase, PDB code: 1wzg was solved by M.Unno, N.Yokoi, T.Ueno, Y.Watanabe, M.Ikeda-Saito, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.75
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 41.471, 62.884, 77.991, 90.00, 98.89, 90.00
R / Rfree (%) 17.1 / 21.5

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of An Artificial Metalloprotein: Fe(Salophen)/Wild Type Heme Oxygenase (pdb code 1wzg). 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 Structure of An Artificial Metalloprotein: Fe(Salophen)/Wild Type Heme Oxygenase, PDB code: 1wzg:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 1wzg

Go back to Iron Binding Sites List in 1wzg
Iron binding site 1 out of 2 in the Crystal Structure of An Artificial Metalloprotein: Fe(Salophen)/Wild Type Heme Oxygenase


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 An Artificial Metalloprotein: Fe(Salophen)/Wild Type Heme Oxygenase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe901

b:26.8
occ:1.00
FE A:YOM901 0.0 26.8 1.0
OB A:YOM901 2.0 25.3 1.0
NA A:YOM901 2.1 29.9 1.0
OA A:YOM901 2.1 36.6 1.0
NB A:YOM901 2.2 25.9 1.0
NE2 A:HIS20 2.2 22.4 1.0
OE1 A:GLU24 2.3 31.4 1.0
CC1 A:YOM901 3.0 30.0 1.0
CC2 A:YOM901 3.0 26.5 1.0
CA A:YOM901 3.0 35.0 1.0
CB A:YOM901 3.0 28.3 1.0
CB2 A:YOM901 3.0 27.6 1.0
CA2 A:YOM901 3.1 39.8 1.0
CE1 A:HIS20 3.2 22.5 1.0
CD2 A:HIS20 3.2 21.4 1.0
CD A:GLU24 3.3 26.5 1.0
CA1 A:YOM901 3.4 38.7 1.0
CB1 A:YOM901 3.5 28.5 1.0
CG A:GLU24 3.8 26.5 1.0
ND1 A:HIS20 4.3 21.0 1.0
CB3 A:YOM901 4.3 33.0 1.0
CG A:HIS20 4.3 19.9 1.0
CC6 A:YOM901 4.3 31.6 1.0
CA3 A:YOM901 4.4 45.7 1.0
O A:HOH1088 4.4 40.5 1.0
CC3 A:YOM901 4.4 28.0 1.0
OE2 A:GLU24 4.4 30.0 1.0
CB A:GLU24 4.7 23.6 1.0
CE2 A:PHE201 4.8 14.6 1.0
CA6 A:YOM901 4.8 42.6 1.0
CB6 A:YOM901 4.9 33.0 1.0
O A:HOH1051 5.0 44.4 1.0

Iron binding site 2 out of 2 in 1wzg

Go back to Iron Binding Sites List in 1wzg
Iron binding site 2 out of 2 in the Crystal Structure of An Artificial Metalloprotein: Fe(Salophen)/Wild Type Heme Oxygenase


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 An Artificial Metalloprotein: Fe(Salophen)/Wild Type Heme Oxygenase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe902

b:27.9
occ:1.00
FE B:YOM902 0.0 27.9 1.0
OB B:YOM902 2.0 28.7 1.0
NA B:YOM902 2.1 32.7 1.0
OA B:YOM902 2.1 36.8 1.0
NB B:YOM902 2.2 25.9 1.0
NE2 B:HIS20 2.2 16.4 1.0
OE2 B:GLU24 2.3 27.8 1.0
CC1 B:YOM902 3.0 33.8 1.0
CC2 B:YOM902 3.0 28.7 1.0
CA B:YOM902 3.0 40.6 1.0
CB2 B:YOM902 3.0 28.2 1.0
CB B:YOM902 3.0 24.0 1.0
CA2 B:YOM902 3.1 42.9 1.0
CD2 B:HIS20 3.1 17.3 1.0
CD B:GLU24 3.2 28.3 1.0
CE1 B:HIS20 3.3 20.8 1.0
CG B:GLU24 3.4 27.3 1.0
CA1 B:YOM902 3.4 46.3 1.0
CB1 B:YOM902 3.4 24.8 1.0
CB3 B:YOM902 4.3 35.0 1.0
OE1 B:GLU24 4.3 32.9 1.0
CG B:HIS20 4.3 18.2 1.0
CC3 B:YOM902 4.3 31.9 1.0
CC6 B:YOM902 4.3 45.5 1.0
ND1 B:HIS20 4.4 19.6 1.0
CA3 B:YOM902 4.4 50.7 1.0
CE2 B:PHE201 4.7 13.0 1.0
CA6 B:YOM902 4.8 56.1 1.0
CB6 B:YOM902 4.8 29.6 1.0
CB B:GLU24 4.9 26.6 1.0

Reference:

T.Ueno, N.Yokoi, M.Unno, T.Matsui, Y.Tokita, M.Yamada, M.Ikeda-Saito, H.Nakajima, Y.Watanabe. Design of Metal Cofactors Activated By A Protein-Protein Electron Transfer System. Proc.Natl.Acad.Sci.Usa V. 103 9416 2006.
ISSN: ISSN 0027-8424
PubMed: 16769893
DOI: 10.1073/PNAS.0510968103
Page generated: Wed Jul 16 22:01:12 2025

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