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Iron in PDB 2yl3: Cytochrome C Prime From Alcaligenes Xylosoxidans: Carbon Monooxide Bound L16G Variant at 1.04 A Resolution - Restraint Refined

Protein crystallography data

The structure of Cytochrome C Prime From Alcaligenes Xylosoxidans: Carbon Monooxide Bound L16G Variant at 1.04 A Resolution - Restraint Refined, PDB code: 2yl3 was solved by S.V.Antonyuk, N.Rustage, 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) 46.34 / 1.04
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 53.506, 53.506, 181.574, 90.00, 90.00, 120.00
R / Rfree (%) 12.5 / 14.6

Iron Binding Sites:

The binding sites of Iron atom in the Cytochrome C Prime From Alcaligenes Xylosoxidans: Carbon Monooxide Bound L16G Variant at 1.04 A Resolution - Restraint Refined (pdb code 2yl3). 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 L16G Variant at 1.04 A Resolution - Restraint Refined, PDB code: 2yl3:

Iron binding site 1 out of 1 in 2yl3

Go back to Iron Binding Sites List in 2yl3
Iron binding site 1 out of 1 in the Cytochrome C Prime From Alcaligenes Xylosoxidans: Carbon Monooxide Bound L16G Variant at 1.04 A Resolution - Restraint Refined


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 L16G Variant at 1.04 A Resolution - Restraint Refined within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1128

b:6.3
occ:1.00
FE A:HEC1128 0.0 6.3 1.0
C A:CMO1127 1.9 7.8 1.0
NC A:HEC1128 2.0 6.5 1.0
NB A:HEC1128 2.0 6.4 1.0
ND A:HEC1128 2.0 6.7 1.0
NA A:HEC1128 2.0 7.2 1.0
NE2 A:HIS120 2.1 7.5 1.0
O A:CMO1127 3.0 9.0 1.0
CE1 A:HIS120 3.0 7.8 1.0
C1C A:HEC1128 3.0 5.9 1.0
C1D A:HEC1128 3.1 6.6 1.0
C4B A:HEC1128 3.1 6.1 1.0
C1B A:HEC1128 3.1 6.7 1.0
C4C A:HEC1128 3.1 6.1 1.0
C1A A:HEC1128 3.1 7.7 1.0
C4A A:HEC1128 3.1 6.8 1.0
C4D A:HEC1128 3.1 6.8 1.0
CD2 A:HIS120 3.1 7.3 1.0
HE1 A:HIS120 3.2 7.7 1.0
HD2 A:HIS120 3.3 7.3 1.0
CHC A:HEC1128 3.4 6.3 1.0
CHB A:HEC1128 3.4 7.7 1.0
CHA A:HEC1128 3.4 7.7 1.0
CHD A:HEC1128 3.4 7.1 1.0
HH11 A:ARG124 4.1 11.0 1.0
ND1 A:HIS120 4.2 8.4 1.0
CG A:HIS120 4.2 8.0 1.0
C2A A:HEC1128 4.3 8.7 1.0
C3B A:HEC1128 4.3 6.7 1.0
C3A A:HEC1128 4.3 8.3 1.0
C2B A:HEC1128 4.3 6.8 1.0
C2D A:HEC1128 4.3 6.9 1.0
C2C A:HEC1128 4.3 6.4 1.0
C3D A:HEC1128 4.3 7.0 1.0
C3C A:HEC1128 4.3 6.5 1.0
HH2 A:TRP56 4.3 7.6 1.0
HHC A:HEC1128 4.4 6.1 1.0
HHB A:HEC1128 4.4 7.4 1.0
HHA A:HEC1128 4.4 7.4 1.0
HHD A:HEC1128 4.4 6.8 1.0
HD3 A:ARG124 4.5 10.4 1.0
CE A:MET19 4.6 8.3 0.7
NH1 A:ARG124 4.6 11.2 1.0
HA3 A:GLY16 4.6 6.8 1.0
HA2 A:GLY16 4.6 6.8 1.0
HH12 A:ARG124 4.7 10.9 1.0
HD1 A:HIS120 4.9 8.0 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 06:13:28 2025

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