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Iron in PDB 2icv: 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: 2icv 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 / 1.60
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 43.958, 52.477, 136.250, 90.00, 90.00, 90.00
R / Rfree (%) 22.3 / 25.7

Other elements in 2icv:

The structure of Kinetic and Crystallographic Studies of A Redesigned Manganese-Binding Site in Cytochrome C Peroxidase also contains other interesting chemical elements:

Cobalt (Co) 1 atom

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 2icv). 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: 2icv:

Iron binding site 1 out of 1 in 2icv

Go back to Iron Binding Sites List in 2icv
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:14.2
occ:1.00
 FE A:HEM296 0.0 14.2 1.0
ND A:HEM296 2.0 13.0 1.0
NB A:HEM296 2.0 11.2 1.0
NC A:HEM296 2.0 21.2 1.0
NA A:HEM296 2.0 22.5 1.0
NE2 A:HIS175 2.1 18.2 1.0
C4B A:HEM296 3.0 13.0 1.0
C4D A:HEM296 3.0 18.9 1.0
C1D A:HEM296 3.0 16.6 1.0
C1A A:HEM296 3.0 20.5 1.0
C1B A:HEM296 3.1 15.1 1.0
C1C A:HEM296 3.1 12.5 1.0
C4A A:HEM296 3.1 13.6 1.0
C4C A:HEM296 3.1 15.6 1.0
CE1 A:HIS175 3.1 17.6 1.0
CD2 A:HIS175 3.1 19.2 1.0
CHA A:HEM296 3.4 24.3 1.0
CHD A:HEM296 3.4 21.1 1.0
CHC A:HEM296 3.4 19.0 1.0
CHB A:HEM296 3.5 15.3 1.0
NE1 A:TRP51 4.2 16.0 1.0
C3D A:HEM296 4.2 13.6 1.0
C2D A:HEM296 4.2 16.1 1.0
ND1 A:HIS175 4.2 17.4 1.0
C3B A:HEM296 4.3 16.0 1.0
C2A A:HEM296 4.3 24.3 1.0
C2B A:HEM296 4.3 15.6 1.0
C3A A:HEM296 4.3 24.9 1.0
CG A:HIS175 4.3 19.5 1.0
C2C A:HEM296 4.3 13.8 1.0
C3C A:HEM296 4.3 15.4 1.0
CD1 A:TRP51 4.6 20.6 1.0
NE A:ARG48 4.8 17.7 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: Sat Aug 3 23:20:27 2024

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