Atomistry » Iron » PDB 1gem-1gwe » 1gqa
Atomistry »
  Iron »
    PDB 1gem-1gwe »
      1gqa »

Iron in PDB 1gqa: Cytochrome C' From Rhodobacter Spheriodes

Protein crystallography data

The structure of Cytochrome C' From Rhodobacter Spheriodes, PDB code: 1gqa was solved by K.A.Kantardjieff, B.Rupp, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.00 / 1.80
Space group P 31
Cell size a, b, c (Å), α, β, γ (°) 48.100, 48.100, 115.798, 90.00, 90.00, 120.00
R / Rfree (%) 20.5 / 25.4

Iron Binding Sites:

The binding sites of Iron atom in the Cytochrome C' From Rhodobacter Spheriodes (pdb code 1gqa). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Cytochrome C' From Rhodobacter Spheriodes, PDB code: 1gqa:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 1gqa

Go back to Iron Binding Sites List in 1gqa
Iron binding site 1 out of 2 in the Cytochrome C' From Rhodobacter Spheriodes


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cytochrome C' From Rhodobacter Spheriodes within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe131

b:13.5
occ:1.00
FE A:HEC131 0.0 13.5 1.0
NE2 A:HIS123 1.9 13.0 1.0
NC A:HEC131 2.1 12.7 1.0
NB A:HEC131 2.2 11.2 1.0
NA A:HEC131 2.2 14.3 1.0
ND A:HEC131 2.3 13.1 1.0
CE1 A:HIS123 2.9 13.4 1.0
CD2 A:HIS123 3.0 14.6 1.0
C4A A:HEC131 3.1 14.2 1.0
C1A A:HEC131 3.1 15.6 1.0
C4D A:HEC131 3.1 12.5 1.0
C1C A:HEC131 3.1 11.3 1.0
C1D A:HEC131 3.1 13.2 1.0
C4C A:HEC131 3.1 13.1 1.0
C1B A:HEC131 3.2 11.9 1.0
C4B A:HEC131 3.2 11.8 1.0
CD1 A:PHE14 3.4 14.4 1.0
CHA A:HEC131 3.4 14.7 1.0
CHD A:HEC131 3.4 12.4 1.0
CHB A:HEC131 3.4 14.6 1.0
CHC A:HEC131 3.4 10.7 1.0
CE1 A:PHE14 3.6 15.6 1.0
CG A:PHE14 4.0 14.0 1.0
ND1 A:HIS123 4.0 14.9 1.0
CG A:HIS123 4.1 13.9 1.0
C2A A:HEC131 4.3 17.2 1.0
C3A A:HEC131 4.3 16.9 1.0
C3C A:HEC131 4.3 12.1 1.0
C2C A:HEC131 4.3 12.0 1.0
C3D A:HEC131 4.3 13.3 1.0
C2D A:HEC131 4.3 13.4 1.0
C2B A:HEC131 4.4 11.7 1.0
C3B A:HEC131 4.4 9.8 1.0
CZ A:PHE14 4.4 13.6 1.0
NH2 A:ARG127 4.5 19.5 1.0
CB A:PHE14 4.6 13.6 1.0
CD2 A:PHE14 4.7 14.4 1.0
CE2 A:PHE14 4.9 13.8 1.0

Iron binding site 2 out of 2 in 1gqa

Go back to Iron Binding Sites List in 1gqa
Iron binding site 2 out of 2 in the Cytochrome C' From Rhodobacter Spheriodes


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Cytochrome C' From Rhodobacter Spheriodes within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe131

b:14.2
occ:1.00
FE D:HEC131 0.0 14.2 1.0
NE2 D:HIS123 2.0 13.4 1.0
NC D:HEC131 2.1 13.5 1.0
NB D:HEC131 2.2 13.2 1.0
NA D:HEC131 2.2 14.2 1.0
ND D:HEC131 2.2 12.6 1.0
CE1 D:HIS123 2.9 11.0 1.0
C1D D:HEC131 3.1 12.8 1.0
C4D D:HEC131 3.1 12.9 1.0
C4C D:HEC131 3.1 12.7 1.0
CD2 D:HIS123 3.1 13.2 1.0
C1C D:HEC131 3.1 10.8 1.0
C4A D:HEC131 3.1 14.2 1.0
C1A D:HEC131 3.1 15.7 1.0
C1B D:HEC131 3.1 12.4 1.0
C4B D:HEC131 3.2 12.7 1.0
CD1 D:PHE14 3.2 14.7 1.0
CHD D:HEC131 3.4 12.1 1.0
CHC D:HEC131 3.4 12.6 1.0
CHB D:HEC131 3.4 13.7 1.0
CHA D:HEC131 3.5 14.9 1.0
CE1 D:PHE14 3.5 14.6 1.0
CG D:PHE14 3.8 14.6 1.0
ND1 D:HIS123 4.1 13.1 1.0
CG D:HIS123 4.2 14.7 1.0
CZ D:PHE14 4.2 13.2 1.0
C3C D:HEC131 4.3 12.6 1.0
C3D D:HEC131 4.3 13.5 1.0
C2C D:HEC131 4.3 13.5 1.0
C2D D:HEC131 4.3 12.6 1.0
C2A D:HEC131 4.3 17.4 1.0
C3A D:HEC131 4.3 16.9 1.0
C3B D:HEC131 4.3 11.3 1.0
C2B D:HEC131 4.3 12.1 1.0
CB D:PHE14 4.4 13.3 1.0
CD2 D:PHE14 4.5 14.5 1.0
CE2 D:PHE14 4.7 14.5 1.0
NH2 D:ARG127 4.8 23.7 1.0

Reference:

L.M.Ramirez, H.L.Axelrod, S.R.Herron, B.Rupp, J.P.Allen, K.A.Kantardjieff. High Resolution Crystal Structure of Ferricytochrome C' From Rhodobacter Sphaeroides J.Chem.Cryst. V. 33 413 2003.
ISSN: ISSN 1074-1542
Page generated: Sat Aug 3 06:15:54 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