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Iron in PDB 1wzf: Crystal Structure of An Artificial Metalloprotein: Fe(10-Cooh- Salophen)/Wild Type Heme Oxygenase

Enzymatic activity of Crystal Structure of An Artificial Metalloprotein: Fe(10-Cooh- Salophen)/Wild Type Heme Oxygenase

All present enzymatic activity of Crystal Structure of An Artificial Metalloprotein: Fe(10-Cooh- Salophen)/Wild Type Heme Oxygenase:
1.14.99.3;

Protein crystallography data

The structure of Crystal Structure of An Artificial Metalloprotein: Fe(10-Cooh- Salophen)/Wild Type Heme Oxygenase, PDB code: 1wzf 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 / 1.85
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 40.810, 62.875, 77.693, 90.00, 97.93, 90.00
R / Rfree (%) 18.2 / 23.5

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of An Artificial Metalloprotein: Fe(10-Cooh- Salophen)/Wild Type Heme Oxygenase (pdb code 1wzf). 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(10-Cooh- Salophen)/Wild Type Heme Oxygenase, PDB code: 1wzf:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 1wzf

Go back to Iron Binding Sites List in 1wzf
Iron binding site 1 out of 2 in the Crystal Structure of An Artificial Metalloprotein: Fe(10-Cooh- 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(10-Cooh- Salophen)/Wild Type Heme Oxygenase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe901

b:46.4
occ:1.00
FE A:YOL901 0.0 46.4 1.0
OA A:YOL901 2.0 52.8 1.0
OB A:YOL901 2.0 46.3 1.0
NE2 A:HIS20 2.2 33.9 1.0
NA A:YOL901 2.2 46.1 1.0
NB A:YOL901 2.2 39.6 1.0
OE2 A:GLU24 2.4 43.4 1.0
CC2 A:YOL901 3.0 40.4 1.0
CC1 A:YOL901 3.0 44.2 1.0
CB2 A:YOL901 3.0 42.9 1.0
CA A:YOL901 3.1 49.5 1.0
CD2 A:HIS20 3.1 33.8 1.0
CB A:YOL901 3.1 37.7 1.0
CA2 A:YOL901 3.1 55.8 1.0
CE1 A:HIS20 3.2 36.3 1.0
CD A:GLU24 3.3 38.7 1.0
CB1 A:YOL901 3.5 39.5 1.0
CG A:GLU24 3.5 37.5 1.0
CA1 A:YOL901 3.6 53.8 1.0
CG A:HIS20 4.2 32.5 1.0
ND1 A:HIS20 4.3 36.0 1.0
CC3 A:YOL901 4.3 38.4 1.0
CB3 A:YOL901 4.3 46.6 1.0
CC6 A:YOL901 4.3 45.8 1.0
CA3 A:YOL901 4.4 62.6 1.0
OE1 A:GLU24 4.5 41.3 1.0
CE2 A:PHE201 4.5 27.5 1.0
CB A:GLU24 4.9 35.6 1.0
CB6 A:YOL901 4.9 38.9 1.0
CA6 A:YOL901 5.0 57.3 1.0

Iron binding site 2 out of 2 in 1wzf

Go back to Iron Binding Sites List in 1wzf
Iron binding site 2 out of 2 in the Crystal Structure of An Artificial Metalloprotein: Fe(10-Cooh- 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(10-Cooh- Salophen)/Wild Type Heme Oxygenase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe902

b:23.5
occ:1.00
FE B:YOL902 0.0 23.5 1.0
OA B:YOL902 2.0 27.8 1.0
OB B:YOL902 2.0 21.9 1.0
NA B:YOL902 2.2 21.4 1.0
OE2 B:GLU24 2.2 27.1 1.0
NB B:YOL902 2.3 18.7 1.0
NE2 B:HIS20 2.3 20.1 1.0
CC1 B:YOL902 2.9 22.1 1.0
CC2 B:YOL902 2.9 20.0 1.0
CB2 B:YOL902 3.0 22.7 1.0
CA B:YOL902 3.1 24.4 1.0
CD B:GLU24 3.1 34.5 1.0
CA2 B:YOL902 3.1 27.2 1.0
CD2 B:HIS20 3.1 19.9 1.0
CB B:YOL902 3.1 18.5 1.0
CG B:GLU24 3.3 29.0 1.0
CE1 B:HIS20 3.3 22.4 1.0
CB1 B:YOL902 3.4 20.8 1.0
CA1 B:YOL902 3.5 26.3 1.0
CB3 B:YOL902 4.2 24.7 1.0
CC6 B:YOL902 4.2 22.1 1.0
CC3 B:YOL902 4.2 22.0 1.0
OE1 B:GLU24 4.3 40.5 1.0
CA3 B:YOL902 4.3 31.1 1.0
CG B:HIS20 4.3 20.7 1.0
ND1 B:HIS20 4.4 18.8 1.0
CB B:GLU24 4.8 28.4 1.0
CB6 B:YOL902 4.9 21.8 1.0
CE2 B:PHE201 4.9 16.2 1.0
CA6 B:YOL902 4.9 27.7 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: Sun Dec 13 14:35:28 2020

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