Atomistry » Iron » PDB 4cuo-4d36 » 4cvj
Atomistry »
  Iron »
    PDB 4cuo-4d36 »
      4cvj »

Iron in PDB 4cvj: Neutron Structure of Compound I Intermediate of Cytochrome C Peroxidase - Deuterium Exchanged 100 K

Enzymatic activity of Neutron Structure of Compound I Intermediate of Cytochrome C Peroxidase - Deuterium Exchanged 100 K

All present enzymatic activity of Neutron Structure of Compound I Intermediate of Cytochrome C Peroxidase - Deuterium Exchanged 100 K:
1.11.1.5;

Protein crystallography data

The structure of Neutron Structure of Compound I Intermediate of Cytochrome C Peroxidase - Deuterium Exchanged 100 K, PDB code: 4cvj was solved by C.M.Casadei, A.Gumiero, M.P.Blakeley, A.Ostermann, E.L.Raven, P.C.E.Moody, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 2.50
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 51.190, 75.830, 107.590, 90.00, 90.00, 90.00
R / Rfree (%) 18.73 / 27.2

Iron Binding Sites:

The binding sites of Iron atom in the Neutron Structure of Compound I Intermediate of Cytochrome C Peroxidase - Deuterium Exchanged 100 K (pdb code 4cvj). 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 Neutron Structure of Compound I Intermediate of Cytochrome C Peroxidase - Deuterium Exchanged 100 K, PDB code: 4cvj:

Iron binding site 1 out of 1 in 4cvj

Go back to Iron Binding Sites List in 4cvj
Iron binding site 1 out of 1 in the Neutron Structure of Compound I Intermediate of Cytochrome C Peroxidase - Deuterium Exchanged 100 K


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Neutron Structure of Compound I Intermediate of Cytochrome C Peroxidase - Deuterium Exchanged 100 K within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1295

b:15.4
occ:1.00
FE A:HEM1295 0.0 15.4 1.0
O A:DOD2081 1.6 16.9 1.0
NA A:HEM1295 2.0 13.0 1.0
NB A:HEM1295 2.0 14.1 1.0
NC A:HEM1295 2.1 16.1 1.0
ND A:HEM1295 2.1 13.4 1.0
NE2 A:HIS175 2.1 11.7 1.0
D2 A:DOD2085 3.0 13.9 1.0
C1A A:HEM1295 3.0 13.7 1.0
C4A A:HEM1295 3.0 18.8 1.0
DE A:ARG48 3.0 17.3 1.0
C4B A:HEM1295 3.0 11.5 1.0
C1C A:HEM1295 3.0 12.5 1.0
CE1 A:HIS175 3.0 15.7 1.0
C4C A:HEM1295 3.1 14.7 1.0
C1D A:HEM1295 3.1 13.2 1.0
C4D A:HEM1295 3.1 15.0 1.0
C1B A:HEM1295 3.1 15.3 1.0
DE1 A:TRP51 3.1 14.6 0.7
HE1 A:TRP51 3.1 14.6 0.3
CD2 A:HIS175 3.2 11.8 1.0
HE1 A:HIS175 3.2 14.2 1.0
HD2 A:HIS175 3.4 14.0 1.0
CHC A:HEM1295 3.4 12.9 1.0
CHA A:HEM1295 3.4 13.3 1.0
CHD A:HEM1295 3.4 13.3 1.0
CHB A:HEM1295 3.4 11.0 1.0
DH21 A:ARG48 3.6 18.7 1.0
NE A:ARG48 3.8 17.8 1.0
NE1 A:TRP51 3.9 14.6 1.0
O A:DOD2085 3.9 13.9 1.0
HG3 A:ARG48 3.9 15.7 1.0
C2A A:HEM1295 4.2 15.7 1.0
ND1 A:HIS175 4.2 12.6 1.0
C3A A:HEM1295 4.2 21.2 1.0
C3C A:HEM1295 4.3 15.1 1.0
C2C A:HEM1295 4.3 13.7 1.0
C3B A:HEM1295 4.3 12.0 1.0
CG A:HIS175 4.3 13.2 1.0
HHD A:HEM1295 4.3 11.8 1.0
C2B A:HEM1295 4.3 14.0 1.0
C2D A:HEM1295 4.3 14.0 1.0
D1 A:DOD2085 4.3 13.9 1.0
HD1 A:TRP51 4.3 13.1 1.0
C3D A:HEM1295 4.3 13.4 1.0
HHA A:HEM1295 4.3 13.2 1.0
NH2 A:ARG48 4.3 17.4 1.0
HHC A:HEM1295 4.4 13.3 1.0
HHB A:HEM1295 4.4 16.8 1.0
CD1 A:TRP51 4.5 14.2 1.0
HE2 A:HIS52 4.5 16.6 0.2
DE2 A:HIS52 4.5 16.6 0.8
CZ A:ARG48 4.6 16.5 1.0
HH2 A:TRP191 4.6 17.3 1.0
HD2 A:ARG48 4.6 15.2 1.0
CD A:ARG48 4.7 15.2 1.0
CG A:ARG48 4.8 14.3 1.0
CE2 A:TRP51 4.9 18.2 1.0
HD1 A:HIS175 5.0 13.9 0.3
DD1 A:HIS175 5.0 13.9 0.7

Reference:

C.M.Casadei, A.Gumiero, C.L.Metcalfe, E.J.Murphy, J.Basran, M.G.Concilio, S.C.M.Teixeira, T.E.Schrader, A.J.Fielding, A.Ostermann, M.P.Blakeley, E.L.Raven, P.C.E.Moody. Neutron Cryo-Crystallography Captures the Protonation State of Ferryl Heme in A Peroxidase Science V. 345 193 2014.
ISSN: ISSN 0036-8075
PubMed: 25013070
DOI: 10.1126/SCIENCE.1254398
Page generated: Mon Aug 5 00:57:12 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy