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Iron in PDB 4gpf: Structure of the FE3+-Biliverdin-Hmuo, Heme Oxygenase From Corynebacterium Diphtheriae (Data Set III)

Enzymatic activity of Structure of the FE3+-Biliverdin-Hmuo, Heme Oxygenase From Corynebacterium Diphtheriae (Data Set III)

All present enzymatic activity of Structure of the FE3+-Biliverdin-Hmuo, Heme Oxygenase From Corynebacterium Diphtheriae (Data Set III):
1.14.99.3;

Protein crystallography data

The structure of Structure of the FE3+-Biliverdin-Hmuo, Heme Oxygenase From Corynebacterium Diphtheriae (Data Set III), PDB code: 4gpf was solved by M.Unno, M.Ikeda-Saito, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.90
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 53.937, 62.539, 107.589, 90.00, 101.09, 90.00
R / Rfree (%) 18.5 / 23.9

Iron Binding Sites:

The binding sites of Iron atom in the Structure of the FE3+-Biliverdin-Hmuo, Heme Oxygenase From Corynebacterium Diphtheriae (Data Set III) (pdb code 4gpf). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Structure of the FE3+-Biliverdin-Hmuo, Heme Oxygenase From Corynebacterium Diphtheriae (Data Set III), PDB code: 4gpf:

Iron binding site 1 out of 1 in 4gpf

Go back to Iron Binding Sites List in 4gpf
Iron binding site 1 out of 1 in the Structure of the FE3+-Biliverdin-Hmuo, Heme Oxygenase From Corynebacterium Diphtheriae (Data Set III)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of the FE3+-Biliverdin-Hmuo, Heme Oxygenase From Corynebacterium Diphtheriae (Data Set III) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe902

b:41.5
occ:1.00
 NA A:BLA901 2.0 36.1 1.0
NB A:BLA901 2.1 30.3 1.0
NE2 A:HIS20 2.1 40.7 1.0
NC A:BLA901 2.2 49.9 1.0
ND A:BLA901 2.3 43.2 1.0
C4A A:BLA901 3.0 33.8 1.0
C1B A:BLA901 3.0 29.2 1.0
CE1 A:HIS20 3.1 41.3 1.0
C4B A:BLA901 3.1 33.5 1.0
C1A A:BLA901 3.1 42.1 1.0
CD2 A:HIS20 3.1 42.1 1.0
C1C A:BLA901 3.1 49.5 1.0
C4C A:BLA901 3.2 49.0 1.0
C4D A:BLA901 3.2 44.9 1.0
C1D A:BLA901 3.3 48.1 1.0
CHB A:BLA901 3.3 33.7 1.0
OB A:BLA901 3.3 36.4 1.0
OC A:BLA901 3.4 49.3 1.0
CHD A:BLA901 3.5 46.6 1.0
CHA A:BLA901 3.5 40.6 1.0
ND1 A:HIS20 4.2 44.2 1.0
CG A:HIS20 4.3 41.3 1.0
C3B A:BLA901 4.3 34.8 1.0
C3A A:BLA901 4.3 34.5 1.0
C2B A:BLA901 4.3 31.9 1.0
C2A A:BLA901 4.4 35.5 1.0
C3C A:BLA901 4.4 48.7 1.0
C2C A:BLA901 4.4 48.8 1.0
C3D A:BLA901 4.6 45.8 1.0
C2D A:BLA901 4.6 46.7 1.0
CA A:GLY135 4.7 25.4 1.0
O A:HOH1062 4.7 35.4 1.0
O A:GLY135 5.0 24.8 1.0

Reference:

M.Unno, A.Ardevol, C.Rovira, M.Ikeda-Saito. Crystal Structure of the Substrate-Free and the Product-Bound Forms of Hmuo, A Heme Oxygenase From Corynebacterium Diphtheriae To Be Published.
Page generated: Sun Dec 13 15:35:42 2020

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