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Iron in PDB 3a4h: Structure of Cytochrome P450 Vdh From Pseudonocardia Autotrophica (Orthorhombic Crystal Form)

Protein crystallography data

The structure of Structure of Cytochrome P450 Vdh From Pseudonocardia Autotrophica (Orthorhombic Crystal Form), PDB code: 3a4h was solved by Y.Yasutake, Y.Fujii, W.K.Cheon, A.Arisawa, T.Tamura, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.74 / 3.06
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 63.595, 65.793, 102.264, 90.00, 90.00, 90.00
R / Rfree (%) 21.7 / 27

Other elements in 3a4h:

The structure of Structure of Cytochrome P450 Vdh From Pseudonocardia Autotrophica (Orthorhombic Crystal Form) also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Structure of Cytochrome P450 Vdh From Pseudonocardia Autotrophica (Orthorhombic Crystal Form) (pdb code 3a4h). 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 Cytochrome P450 Vdh From Pseudonocardia Autotrophica (Orthorhombic Crystal Form), PDB code: 3a4h:

Iron binding site 1 out of 1 in 3a4h

Go back to Iron Binding Sites List in 3a4h
Iron binding site 1 out of 1 in the Structure of Cytochrome P450 Vdh From Pseudonocardia Autotrophica (Orthorhombic Crystal Form)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Cytochrome P450 Vdh From Pseudonocardia Autotrophica (Orthorhombic Crystal Form) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe412

b:31.5
occ:1.00
FE A:HEM412 0.0 31.5 1.0
NA A:HEM412 2.0 31.1 1.0
NB A:HEM412 2.1 31.3 1.0
ND A:HEM412 2.1 31.3 1.0
NC A:HEM412 2.1 31.2 1.0
SG A:CYS347 2.4 33.0 1.0
C4A A:HEM412 3.0 31.5 1.0
C1A A:HEM412 3.0 30.9 1.0
C1B A:HEM412 3.1 31.4 1.0
C4D A:HEM412 3.1 31.2 1.0
C1D A:HEM412 3.1 31.2 1.0
C4C A:HEM412 3.1 31.4 1.0
C4B A:HEM412 3.1 31.4 1.0
C1C A:HEM412 3.1 31.5 1.0
CHB A:HEM412 3.4 31.4 1.0
CHA A:HEM412 3.4 31.2 1.0
CB A:CYS347 3.4 33.1 1.0
CHD A:HEM412 3.4 31.4 1.0
CHC A:HEM412 3.5 31.4 1.0
CA A:CYS347 4.0 33.2 1.0
C3A A:HEM412 4.2 31.1 1.0
C2A A:HEM412 4.2 30.9 1.0
O A:ALA236 4.3 34.0 1.0
C2B A:HEM412 4.3 31.3 1.0
C3B A:HEM412 4.3 31.6 1.0
C3C A:HEM412 4.3 31.4 1.0
C2C A:HEM412 4.3 31.6 1.0
C3D A:HEM412 4.3 31.1 1.0
C2D A:HEM412 4.3 30.9 1.0
CB A:ALA236 4.5 34.4 1.0
C A:CYS347 4.7 33.2 1.0
N A:LEU348 4.7 33.4 1.0
C A:ALA236 4.9 34.1 1.0
N A:GLY349 4.9 33.6 1.0

Reference:

Y.Yasutake, Y.Fujii, T.Nishioka, W.K.Cheon, A.Arisawa, T.Tamura. Structural Evidence For Enhancement of Sequential Vitamin D3 Hydroxylation Activities By Directed Evolution of Cytochrome P450 Vitamin D3 Hydroxylase J.Biol.Chem. V. 285 31193 2010.
ISSN: ISSN 0021-9258
PubMed: 20667833
DOI: 10.1074/JBC.M110.147009
Page generated: Sun Dec 13 14:59:54 2020

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