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

Iron in PDB 4cvi: Neutron Structure of Ferric Cytochrome C Peroxidase - Deuterium Exchanged at Room Temperature

Enzymatic activity of Neutron Structure of Ferric Cytochrome C Peroxidase - Deuterium Exchanged at Room Temperature

All present enzymatic activity of Neutron Structure of Ferric Cytochrome C Peroxidase - Deuterium Exchanged at Room Temperature:
1.11.1.5;

Protein crystallography data

The structure of Neutron Structure of Ferric Cytochrome C Peroxidase - Deuterium Exchanged at Room Temperature, PDB code: 4cvi 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 / 2.41
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 51.700, 76.800, 107.600, 90.00, 90.00, 90.00
R / Rfree (%) 17.59 / 24.33

Iron Binding Sites:

The binding sites of Iron atom in the Neutron Structure of Ferric Cytochrome C Peroxidase - Deuterium Exchanged at Room Temperature (pdb code 4cvi). 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 Ferric Cytochrome C Peroxidase - Deuterium Exchanged at Room Temperature, PDB code: 4cvi:

Iron binding site 1 out of 1 in 4cvi

Go back to Iron Binding Sites List in 4cvi
Iron binding site 1 out of 1 in the Neutron Structure of Ferric Cytochrome C Peroxidase - Deuterium Exchanged at Room Temperature


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 Ferric Cytochrome C Peroxidase - Deuterium Exchanged at Room Temperature within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1295

b:29.7
occ:1.00
 FE A:HEM1295 0.0 29.7 1.0
NE2 A:HIS175 2.0 28.0 1.0
ND A:HEM1295 2.0 26.1 1.0
NB A:HEM1295 2.1 32.3 1.0
NC A:HEM1295 2.1 25.4 1.0
NA A:HEM1295 2.1 30.8 1.0
D1 A:DOD2045 2.3 34.8 0.9
O A:DOD2045 2.7 34.8 0.9
C4D A:HEM1295 3.0 30.0 1.0
CE1 A:HIS175 3.0 28.9 1.0
C1A A:HEM1295 3.0 30.3 1.0
CD2 A:HIS175 3.0 28.3 1.0
C1D A:HEM1295 3.0 25.9 1.0
C4B A:HEM1295 3.0 29.5 1.0
C1C A:HEM1295 3.1 29.2 1.0
C1B A:HEM1295 3.1 30.1 1.0
C4C A:HEM1295 3.1 25.6 1.0
C4A A:HEM1295 3.1 34.0 1.0
HE1 A:HIS175 3.2 30.4 1.0
HD2 A:HIS175 3.2 26.4 1.0
CHA A:HEM1295 3.3 28.8 1.0
CHC A:HEM1295 3.4 24.5 1.0
CHD A:HEM1295 3.5 23.7 1.0
CHB A:HEM1295 3.5 29.4 1.0
D2 A:DOD2045 3.6 34.8 0.9
DE1 A:TRP51 3.7 35.2 1.0
D1 A:DOD2046 3.8 35.1 0.6
ND1 A:HIS175 4.1 27.2 1.0
CG A:HIS175 4.2 29.7 1.0
C3D A:HEM1295 4.2 27.4 1.0
C2D A:HEM1295 4.2 23.7 1.0
O A:DOD2046 4.3 35.1 0.6
C2A A:HEM1295 4.3 31.5 1.0
C3B A:HEM1295 4.3 28.2 1.0
C2B A:HEM1295 4.3 31.2 1.0
HHA A:HEM1295 4.3 31.2 1.0
NE1 A:TRP51 4.3 31.4 1.0
C2C A:HEM1295 4.3 26.2 1.0
C3A A:HEM1295 4.3 32.6 1.0
C3C A:HEM1295 4.3 25.0 1.0
HHC A:HEM1295 4.4 28.9 1.0
HHD A:HEM1295 4.4 26.8 1.0
HD1 A:TRP51 4.4 32.0 1.0
HHB A:HEM1295 4.5 32.9 1.0
HD2 A:ARG48 4.5 32.4 1.0
HH2 A:TRP191 4.5 29.2 1.0
CD1 A:TRP51 4.7 27.6 1.0
HG3 A:ARG48 4.7 33.0 1.0
O A:DOD2041 4.8 41.7 0.7
HZ2 A:TRP191 4.8 31.7 1.0
DD1 A:HIS175 4.9 30.3 1.0
DE A:ARG48 5.0 33.5 1.0

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 9MJ5
Zn in 9HNW
Zn in 9G0L
Zn in 9FNE
Zn in 9DZN
Zn in 9E0I
Zn in 9D32
Zn in 9DAK
Zn in 8ZXC
Zn in 8ZUF
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy