Atomistry » Iron » PDB 1k2r-1kqg » 1kok
Atomistry »
  Iron »
    PDB 1k2r-1kqg »
      1kok »

Iron in PDB 1kok: Crystal Structure of Mesopone Cytochrome C Peroxidase (Mpccp)

Enzymatic activity of Crystal Structure of Mesopone Cytochrome C Peroxidase (Mpccp)

All present enzymatic activity of Crystal Structure of Mesopone Cytochrome C Peroxidase (Mpccp):
1.11.1.5;

Protein crystallography data

The structure of Crystal Structure of Mesopone Cytochrome C Peroxidase (Mpccp), PDB code: 1kok was solved by B.Bhaskar, C.E.Immoos, M.S.Cohen, T.P.Barrows, P.J.Farmer, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 107.011, 76.091, 51.124, 90.00, 90.00, 90.00
R / Rfree (%) 18.6 / 20.7

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Mesopone Cytochrome C Peroxidase (Mpccp) (pdb code 1kok). 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 Crystal Structure of Mesopone Cytochrome C Peroxidase (Mpccp), PDB code: 1kok:

Iron binding site 1 out of 1 in 1kok

Go back to Iron Binding Sites List in 1kok
Iron binding site 1 out of 1 in the Crystal Structure of Mesopone Cytochrome C Peroxidase (Mpccp)


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 Mesopone Cytochrome C Peroxidase (Mpccp) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe296

b:12.2
occ:1.00
FE A:HIF296 0.0 12.2 1.0
O A:HOH916 2.0 14.4 1.0
NC A:HIF296 2.0 12.2 1.0
NB A:HIF296 2.0 12.2 1.0
ND A:HIF296 2.0 12.3 1.0
NA A:HIF296 2.0 11.6 1.0
NE2 A:HIS175 2.1 11.9 1.0
C4C A:HIF296 3.0 12.3 1.0
C1C A:HIF296 3.0 12.3 1.0
C1A A:HIF296 3.1 11.7 1.0
C1D A:HIF296 3.1 11.8 1.0
C4D A:HIF296 3.1 12.0 1.0
C1B A:HIF296 3.1 12.0 1.0
C4B A:HIF296 3.1 11.9 1.0
C4A A:HIF296 3.1 11.9 1.0
CE1 A:HIS175 3.1 12.0 1.0
CD2 A:HIS175 3.1 11.9 1.0
CHA A:HIF296 3.4 11.8 1.0
CHC A:HIF296 3.4 12.0 1.0
CHD A:HIF296 3.5 12.2 1.0
CHB A:HIF296 3.5 12.2 1.0
NE1 A:TRP51 4.0 11.3 1.0
NE A:ARG48 4.1 15.8 1.0
ND1 A:HIS175 4.2 12.3 1.0
CG A:HIS175 4.3 12.1 1.0
C2D A:HIF296 4.3 11.8 1.0
C2A A:HIF296 4.3 11.7 1.0
O A:HOH629 4.3 16.3 1.0
C3D A:HIF296 4.3 11.6 1.0
C2B A:HIF296 4.3 12.2 1.0
C3A A:HIF296 4.3 11.7 1.0
C3B A:HIF296 4.3 12.4 1.0
C2C A:HIF296 4.4 12.6 1.0
C3C A:HIF296 4.4 12.7 1.0
CD1 A:TRP51 4.5 11.5 1.0
NH2 A:ARG48 4.7 15.6 1.0
CBC A:HIF296 4.8 14.8 1.0
CZ A:ARG48 4.9 15.8 1.0
CD A:ARG48 4.9 14.7 1.0
CG A:ARG48 5.0 13.4 1.0

Reference:

C.E.Immoos, B.Bhaskar, M.S.Cohen, T.P.Barrows, P.J.Farmer, T.L.Poulos. Mesopone Cytochrome C Peroxidase: Functional Model of Heme Oxygenated Oxidases. J.Inorg.Biochem. V. 91 635 2002.
ISSN: ISSN 0162-0134
PubMed: 12237229
DOI: 10.1016/S0162-0134(02)00447-6
Page generated: Sun Dec 13 14:21:11 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy