Atomistry » Iron » PDB 4ccx-4cun » 4cjg
Atomistry »
  Iron »
    PDB 4ccx-4cun »
      4cjg »

Iron in PDB 4cjg: Spectroscopically Validated Structure of the 5 Coordinate Proximal No Adduct of Cytochrome C Prime From Alcaligenes Xylosoxidans

Protein crystallography data

The structure of Spectroscopically Validated Structure of the 5 Coordinate Proximal No Adduct of Cytochrome C Prime From Alcaligenes Xylosoxidans, PDB code: 4cjg was solved by D.Kekilli, F.Dworkowski, M.Fuchs, S.Antonyuk, M.A.Hough, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.44 / 1.26
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 53.621, 53.621, 180.259, 90.00, 90.00, 120.00
R / Rfree (%) 16.161 / 19.465

Iron Binding Sites:

The binding sites of Iron atom in the Spectroscopically Validated Structure of the 5 Coordinate Proximal No Adduct of Cytochrome C Prime From Alcaligenes Xylosoxidans (pdb code 4cjg). 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 Spectroscopically Validated Structure of the 5 Coordinate Proximal No Adduct of Cytochrome C Prime From Alcaligenes Xylosoxidans, PDB code: 4cjg:

Iron binding site 1 out of 1 in 4cjg

Go back to Iron Binding Sites List in 4cjg
Iron binding site 1 out of 1 in the Spectroscopically Validated Structure of the 5 Coordinate Proximal No Adduct of Cytochrome C Prime From Alcaligenes Xylosoxidans


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Spectroscopically Validated Structure of the 5 Coordinate Proximal No Adduct of Cytochrome C Prime From Alcaligenes Xylosoxidans within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe128

b:10.3
occ:1.00
FE A:HEC128 0.0 10.3 1.0
N A:NO129 1.8 16.0 1.0
ND A:HEC128 2.0 10.9 1.0
NC A:HEC128 2.0 9.9 1.0
NA A:HEC128 2.0 10.7 1.0
NB A:HEC128 2.0 10.8 1.0
O A:NO129 2.8 27.5 1.0
C1D A:HEC128 3.0 10.4 1.0
C4C A:HEC128 3.0 9.9 1.0
C4A A:HEC128 3.0 10.4 1.0
C1B A:HEC128 3.0 10.3 1.0
C4D A:HEC128 3.0 10.3 1.0
C1C A:HEC128 3.1 9.7 1.0
C1A A:HEC128 3.1 11.4 1.0
C4B A:HEC128 3.1 9.9 1.0
CHD A:HEC128 3.4 11.5 1.0
CHB A:HEC128 3.4 12.0 1.0
CHA A:HEC128 3.4 11.6 1.0
CHC A:HEC128 3.4 10.4 1.0
CD2 A:LEU16 3.7 11.4 1.0
C2D A:HEC128 4.2 11.3 1.0
C3C A:HEC128 4.2 10.3 1.0
C3D A:HEC128 4.2 11.3 1.0
C2B A:HEC128 4.3 10.2 1.0
C2C A:HEC128 4.3 10.1 1.0
C3A A:HEC128 4.3 11.0 1.0
C2A A:HEC128 4.3 11.2 1.0
C3B A:HEC128 4.3 10.5 1.0
CD1 A:LEU16 4.5 10.3 1.0
CG A:LEU16 4.6 9.8 1.0
CB A:LEU16 4.8 8.8 1.0
CD A:ARG124 4.9 16.6 0.3
NH1 A:ARG124 4.9 17.9 0.3

Reference:

D.Kekilli, F.S.Dworkowski, G.Pompidor, M.R.Fuchs, C.R.Andrew, S.Antonyuk, R.W.Strange, R.R.Eady, S.S.Hasnain, M.A.Hough. Fingerprinting Redox and Ligand States in Haemprotein Crystal Structures Using Resonance Raman Spectroscopy. Acta Crystallogr.,Sect.D V. 70 1289 2014.
ISSN: ISSN 0907-4449
PubMed: 24816098
DOI: 10.1107/S1399004714004039
Page generated: Sun Dec 13 15:30:14 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy