Atomistry » Iron » PDB 2xf2-2xuz » 2xlh
Atomistry »
  Iron »
    PDB 2xf2-2xuz »
      2xlh »

Iron in PDB 2xlh: Reduced Structure of R124A Mutant of Cytochrome C' From Alcaligenes Xylosoxidans

Protein crystallography data

The structure of Reduced Structure of R124A Mutant of Cytochrome C' From Alcaligenes Xylosoxidans, PDB code: 2xlh was solved by M.A.Hough, S.V.Antonyuk, S.Barbieri, N.Rustage, A.L.Mckay, A.E.Servid, R.R.Eady, C.R.Andrew, S.S.Hasnain, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.47 / 1.14
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 53.659, 53.659, 181.155, 90.00, 90.00, 120.00
R / Rfree (%) 13.1 / 16.1

Iron Binding Sites:

The binding sites of Iron atom in the Reduced Structure of R124A Mutant of Cytochrome C' From Alcaligenes Xylosoxidans (pdb code 2xlh). 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 Reduced Structure of R124A Mutant of Cytochrome C' From Alcaligenes Xylosoxidans, PDB code: 2xlh:

Iron binding site 1 out of 1 in 2xlh

Go back to Iron Binding Sites List in 2xlh
Iron binding site 1 out of 1 in the Reduced Structure of R124A Mutant of Cytochrome C' 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 Reduced Structure of R124A Mutant of Cytochrome C' From Alcaligenes Xylosoxidans within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe128

b:8.3
occ:1.00
FE A:HEC128 0.0 8.3 1.0
NA A:HEC128 2.1 8.2 1.0
NC A:HEC128 2.1 8.2 1.0
ND A:HEC128 2.1 8.1 1.0
NB A:HEC128 2.1 7.9 1.0
NE2 A:HIS120 2.1 9.6 1.0
C4A A:HEC128 3.1 9.2 1.0
C1B A:HEC128 3.1 9.1 1.0
C1A A:HEC128 3.1 7.9 1.0
C1C A:HEC128 3.1 7.9 1.0
C4B A:HEC128 3.1 8.0 1.0
CD2 A:HIS120 3.1 10.0 1.0
C1D A:HEC128 3.1 7.9 1.0
C4C A:HEC128 3.1 7.5 1.0
C4D A:HEC128 3.1 8.2 1.0
CE1 A:HIS120 3.1 10.7 1.0
CHB A:HEC128 3.4 8.7 1.0
CHA A:HEC128 3.4 8.1 1.0
CHC A:HEC128 3.4 8.0 1.0
CHD A:HEC128 3.4 8.0 1.0
CD2 A:LEU16 3.7 9.2 1.0
ND1 A:HIS120 4.2 12.2 1.0
CG A:HIS120 4.3 10.8 1.0
C3B A:HEC128 4.3 9.1 1.0
C2B A:HEC128 4.3 10.2 1.0
C3A A:HEC128 4.3 8.5 1.0
C2A A:HEC128 4.3 8.8 1.0
C2C A:HEC128 4.3 7.9 1.0
C3C A:HEC128 4.3 7.7 1.0
C3D A:HEC128 4.3 8.5 1.0
C2D A:HEC128 4.3 7.9 1.0
CD1 A:LEU16 4.4 9.1 1.0
CG A:LEU16 4.5 8.1 1.0
O A:HOH2099 4.6 41.2 0.8
CB A:LEU16 4.8 8.0 1.0

Reference:

M.A.Hough, S.V.Antonyuk, S.Barbieri, N.Rustage, A.L.Mckay, A.E.Servid, R.R.Eady, C.R.Andrew, S.S.Hasnain. Distal-to-Proximal No Conversion in Hemoproteins: the Role of the Proximal Pocket. J.Mol.Biol. V. 405 395 2011.
ISSN: ISSN 0022-2836
PubMed: 21073879
DOI: 10.1016/J.JMB.2010.10.035
Page generated: Sun Aug 4 04:38:23 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