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Iron in PDB 2ia8: Kinetic and Crystallographic Studies of A Redesigned Manganese-Binding Site in Cytochrome C Peroxidase

Enzymatic activity of Kinetic and Crystallographic Studies of A Redesigned Manganese-Binding Site in Cytochrome C Peroxidase

All present enzymatic activity of Kinetic and Crystallographic Studies of A Redesigned Manganese-Binding Site in Cytochrome C Peroxidase:
1.11.1.5;

Protein crystallography data

The structure of Kinetic and Crystallographic Studies of A Redesigned Manganese-Binding Site in Cytochrome C Peroxidase, PDB code: 2ia8 was solved by T.Pfister, A.Y.Mirarefi, A.J.Gengenbach, X.Zhao, C.D.N.Conaster, Y.G.Gao, H.Robinson, C.F.Zukoski, A.H.J.Wang, Y.Lu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.48
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 44.192, 52.612, 136.137, 90.00, 90.00, 90.00
R / Rfree (%) 21.2 / 24.7

Iron Binding Sites:

The binding sites of Iron atom in the Kinetic and Crystallographic Studies of A Redesigned Manganese-Binding Site in Cytochrome C Peroxidase (pdb code 2ia8). 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 Kinetic and Crystallographic Studies of A Redesigned Manganese-Binding Site in Cytochrome C Peroxidase, PDB code: 2ia8:

Iron binding site 1 out of 1 in 2ia8

Go back to Iron Binding Sites List in 2ia8
Iron binding site 1 out of 1 in the Kinetic and Crystallographic Studies of A Redesigned Manganese-Binding Site in Cytochrome C Peroxidase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Kinetic and Crystallographic Studies of A Redesigned Manganese-Binding Site in Cytochrome C Peroxidase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe296

b:12.1
occ:1.00
 FE A:HEM296 0.0 12.1 1.0
ND A:HEM296 2.0 12.1 1.0
NB A:HEM296 2.0 13.1 1.0
NC A:HEM296 2.0 12.8 1.0
NA A:HEM296 2.0 15.0 1.0
NE2 A:HIS175 2.1 14.2 1.0
C4D A:HEM296 3.0 14.9 1.0
C4B A:HEM296 3.0 11.8 1.0
C1A A:HEM296 3.0 15.2 1.0
CE1 A:HIS175 3.0 13.0 1.0
C1C A:HEM296 3.0 13.7 1.0
C1D A:HEM296 3.1 11.8 1.0
C4A A:HEM296 3.1 12.1 1.0
C1B A:HEM296 3.1 12.9 1.0
C4C A:HEM296 3.1 12.8 1.0
CD2 A:HIS175 3.1 15.1 1.0
CHA A:HEM296 3.4 10.1 1.0
CHB A:HEM296 3.4 11.6 1.0
CHC A:HEM296 3.4 13.6 1.0
CHD A:HEM296 3.4 11.1 1.0
NE1 A:TRP51 4.1 14.4 1.0
ND1 A:HIS175 4.2 12.8 1.0
CG A:HIS175 4.2 13.8 1.0
C3D A:HEM296 4.2 17.9 1.0
C2D A:HEM296 4.3 16.7 1.0
C3A A:HEM296 4.3 18.4 1.0
C2A A:HEM296 4.3 20.1 1.0
C3C A:HEM296 4.3 17.8 1.0
C2B A:HEM296 4.3 13.5 1.0
C3B A:HEM296 4.3 14.2 1.0
C2C A:HEM296 4.3 14.4 1.0
CD1 A:TRP51 4.6 13.9 1.0
NE A:ARG48 4.8 20.1 1.0

Reference:

T.D.Pfister, A.Y.Mirarefi, A.J.Gengenbach, X.Zhao, C.Danstrom, N.Conatser, Y.-G.Gao, H.Robinson, C.F.Zukoski, A.H.-J.Wang, Y.Lu. Kinetic and Crystallographic Studies of A Redesigned Manganese-Binding Site in Cytochrome C Peroxidase J.Biol.Inorg.Chem. V. 12 126 2007.
ISSN: ISSN 0949-8257
PubMed: 17021923
DOI: 10.1007/S00775-006-0171-0
Page generated: Thu Jul 17 02:13:49 2025

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