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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

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