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Iron in PDB 2yl1: Cytochrome C Prime From Alcaligenes Xylosoxidans: Carbon Monooxide Bound L16A Variant at 1.03 A Resolution - Restraint Refinement

Protein crystallography data

The structure of Cytochrome C Prime From Alcaligenes Xylosoxidans: Carbon Monooxide Bound L16A Variant at 1.03 A Resolution - Restraint Refinement, PDB code: 2yl1 was solved by S.V.Antonyuk, R.R.Eady, S.S.Hasnain, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 32.24 / 1.03
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 53.009, 53.009, 181.114, 90.00, 90.00, 120.00
R / Rfree (%) 13.339 / 14.271

Iron Binding Sites:

The binding sites of Iron atom in the Cytochrome C Prime From Alcaligenes Xylosoxidans: Carbon Monooxide Bound L16A Variant at 1.03 A Resolution - Restraint Refinement (pdb code 2yl1). 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 Cytochrome C Prime From Alcaligenes Xylosoxidans: Carbon Monooxide Bound L16A Variant at 1.03 A Resolution - Restraint Refinement, PDB code: 2yl1:

Iron binding site 1 out of 1 in 2yl1

Go back to Iron Binding Sites List in 2yl1
Iron binding site 1 out of 1 in the Cytochrome C Prime From Alcaligenes Xylosoxidans: Carbon Monooxide Bound L16A Variant at 1.03 A Resolution - Restraint Refinement


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cytochrome C Prime From Alcaligenes Xylosoxidans: Carbon Monooxide Bound L16A Variant at 1.03 A Resolution - Restraint Refinement within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe128

b:7.0
occ:1.00
FE A:HEC128 0.0 7.0 1.0
C A:CMO129 1.8 7.4 1.0
NC A:HEC128 2.0 7.0 1.0
ND A:HEC128 2.0 7.2 1.0
NB A:HEC128 2.0 7.0 1.0
NA A:HEC128 2.0 7.0 1.0
NE2 A:HIS120 2.0 8.1 1.0
O A:CMO129 2.8 11.6 1.0
C1C A:HEC128 3.0 6.8 1.0
CE1 A:HIS120 3.0 8.5 1.0
C4B A:HEC128 3.0 6.9 1.0
C4A A:HEC128 3.0 7.7 1.0
C1A A:HEC128 3.0 7.8 1.0
C1B A:HEC128 3.0 7.5 1.0
C4C A:HEC128 3.0 6.7 1.0
C1D A:HEC128 3.1 7.3 1.0
C4D A:HEC128 3.1 7.1 1.0
CD2 A:HIS120 3.1 7.9 1.0
HE1 A:HIS120 3.2 8.6 1.0
HD2 A:HIS120 3.3 8.2 1.0
CHD A:HEC128 3.4 7.2 1.0
CHC A:HEC128 3.4 7.0 1.0
CHB A:HEC128 3.4 7.9 1.0
CHA A:HEC128 3.4 7.6 1.0
HB3 A:ALA16 3.9 7.7 1.0
HH11 A:ARG124 4.2 11.9 1.0
ND1 A:HIS120 4.2 9.4 1.0
CG A:HIS120 4.2 8.9 1.0
C2D A:HEC128 4.3 7.9 1.0
C3C A:HEC128 4.3 7.1 1.0
C3A A:HEC128 4.3 8.0 1.0
C2B A:HEC128 4.3 8.0 1.0
C3B A:HEC128 4.3 7.7 1.0
C2A A:HEC128 4.3 8.0 1.0
C2C A:HEC128 4.3 7.1 1.0
C3D A:HEC128 4.3 7.9 1.0
HB1 A:ALA16 4.3 7.6 1.0
HHD A:HEC128 4.4 7.1 1.0
HHC A:HEC128 4.4 7.1 1.0
HHB A:HEC128 4.4 7.7 1.0
HH2 A:TRP56 4.4 8.9 1.0
HHA A:HEC128 4.4 7.6 1.0
HD3 A:ARG124 4.5 11.5 1.0
CB A:ALA16 4.6 7.9 1.0
NH1 A:ARG124 4.6 11.7 1.0
CE A:MET19 4.7 9.2 0.5
HH12 A:ARG124 4.7 11.8 1.0
HD1 A:HIS120 4.9 9.1 1.0
HB3 A:CYS116 4.9 9.5 1.0

Reference:

S.V.Antonyuk, N.Rustage, C.A.Petersen, J.L.Arnst, D.J.Heyes, R.Sharma, N.G.Berry, N.S.Scrutton, R.R.Eady, C.R.Andrew, S.S.Hasnain. Carbon Monoxide Poisoning Is Prevented By the Energy Costs of Conformational Changes in Gas- Binding Haemproteins. Proc.Natl.Acad.Sci.Usa V. 108 15780 2011.
ISSN: ISSN 0027-8424
PubMed: 21900609
DOI: 10.1073/PNAS.1109051108
Page generated: Thu Jul 17 06:13:00 2025

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