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Iron in PDB 2wio: Structure of the Histidine Tagged, Open Cytochrome P450 Eryk From S. Erythraea

Protein crystallography data

The structure of Structure of the Histidine Tagged, Open Cytochrome P450 Eryk From S. Erythraea, PDB code: 2wio was solved by C.Savino, L.C.Montemiglio, G.Sciara, A.E.Miele, S.G.Kedrew, S.Gianni, B.Vallone, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 89.80 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 37.932, 57.341, 179.557, 90.00, 90.00, 90.00
R / Rfree (%) 18.341 / 23.202

Iron Binding Sites:

The binding sites of Iron atom in the Structure of the Histidine Tagged, Open Cytochrome P450 Eryk From S. Erythraea (pdb code 2wio). 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 Histidine Tagged, Open Cytochrome P450 Eryk From S. Erythraea, PDB code: 2wio:

Iron binding site 1 out of 1 in 2wio

Go back to Iron Binding Sites List in 2wio
Iron binding site 1 out of 1 in the Structure of the Histidine Tagged, Open Cytochrome P450 Eryk From S. Erythraea


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 Histidine Tagged, Open Cytochrome P450 Eryk From S. Erythraea within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1412

b:17.7
occ:1.00
FE A:HEM1412 0.0 17.7 1.0
NA A:HEM1412 2.0 15.0 1.0
ND A:HEM1412 2.0 17.6 1.0
NC A:HEM1412 2.0 16.7 1.0
NB A:HEM1412 2.1 16.5 1.0
O A:HOH2307 2.3 27.7 1.0
SG A:CYS353 2.3 17.2 1.0
C1A A:HEM1412 3.0 13.2 1.0
C4D A:HEM1412 3.0 15.6 1.0
C1C A:HEM1412 3.0 17.5 1.0
C4C A:HEM1412 3.1 17.1 1.0
C4B A:HEM1412 3.1 16.5 1.0
C1D A:HEM1412 3.1 17.9 1.0
C4A A:HEM1412 3.1 14.6 1.0
C1B A:HEM1412 3.1 17.2 1.0
CHA A:HEM1412 3.3 16.4 1.0
CB A:CYS353 3.4 17.3 1.0
CHC A:HEM1412 3.4 15.8 1.0
CHD A:HEM1412 3.5 16.4 1.0
CHB A:HEM1412 3.5 15.3 1.0
CA A:CYS353 4.0 17.2 1.0
C2A A:HEM1412 4.2 15.0 1.0
O A:HOH2045 4.2 31.7 1.0
C2C A:HEM1412 4.3 16.8 1.0
C3D A:HEM1412 4.3 17.6 1.0
C3C A:HEM1412 4.3 16.1 1.0
C3A A:HEM1412 4.3 12.9 1.0
C2D A:HEM1412 4.3 16.6 1.0
C2B A:HEM1412 4.3 14.0 1.0
C3B A:HEM1412 4.3 13.6 1.0
O A:ALA241 4.4 21.4 1.0
CB A:ALA241 4.5 19.3 1.0
N A:GLY355 4.5 14.9 1.0
N A:LEU354 4.7 17.4 1.0
C A:CYS353 4.7 16.9 1.0
CA A:GLY355 4.9 15.4 1.0

Reference:

C.Savino, L.C.Montemiglio, G.Sciara, A.E.Miele, S.G.Kendrew, P.Jemth, S.Gianni, B.Vallone. Investigating the Structural Plasticity of A Cytochrome P450: Three-Dimensional Structures of P450 Eryk and Binding to Its Physiological Substrate. J.Biol.Chem. V. 284 29170 2009.
ISSN: ISSN 0021-9258
PubMed: 19625248
DOI: 10.1074/JBC.M109.003590
Page generated: Thu Jul 17 05:03:17 2025

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