Chlorine in PDB 4xet: Fe-Cl Bound Y157F Cdo at pH ~7.0 in the Presence of Azide

All present enzymatic activity of Fe-Cl Bound Y157F Cdo at pH ~7.0 in the Presence of Azide:
1.13.11.20;

The structure of Fe-Cl Bound Y157F Cdo at pH ~7.0 in the Presence of Azide, PDB code: 4xet was solved by C.M.Driggers, P.A.Karplus, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.91 / 1.30
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	57.600, 57.600, 122.400, 90.00, 90.00, 90.00
R / Rfree (%)	16.3 / 18.9

The structure of Fe-Cl Bound Y157F Cdo at pH ~7.0 in the Presence of Azide also contains other interesting chemical elements:

Iron

(Fe)

1 atom

The binding sites of Chlorine atom in the Fe-Cl Bound Y157F Cdo at pH ~7.0 in the Presence of Azide (pdb code 4xet). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Fe-Cl Bound Y157F Cdo at pH ~7.0 in the Presence of Azide, PDB code: 4xet:

Chlorine binding site 1 out of 1 in the Fe-Cl Bound Y157F Cdo at pH ~7.0 in the Presence of Azide


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Fe-Cl Bound Y157F Cdo at pH ~7.0 in the Presence of Azide within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl502 b:21.1 occ:1.00 FE A:FE501 2.1 10.3 1.0 O A:HOH601 2.2 7.7 0.3 O A:HOH742 3.3 28.4 1.0 ND1 A:HIS155 3.5 13.5 1.0 NE2 A:HIS140 3.5 12.3 1.0 NE2 A:HIS86 3.5 10.4 1.0 CE1 A:HIS155 3.6 12.4 1.0 NE2 A:HIS88 3.6 12.6 1.0 SG A:CYS93 3.7 17.2 0.8 CE1 A:HIS140 4.0 13.3 1.0 CZ A:PHE157 4.1 18.9 1.0 CE1 A:PHE157 4.1 21.1 1.0 CE1 A:HIS86 4.2 11.7 1.0 CD2 A:HIS88 4.2 12.2 1.0 CD1 A:LEU95 4.6 17.8 1.0 CD2 A:HIS86 4.6 9.6 1.0 CD2 A:HIS140 4.7 11.4 1.0 CE1 A:HIS88 4.8 11.8 1.0 CG A:HIS155 4.8 11.7 1.0 CG2 A:VAL142 4.8 14.5 1.0 NE2 A:HIS155 4.9 12.1 1.0

C.M.Driggers, K.M.Kean, L.L.Hirschberger, R.B.Cooley, M.H.Stipanuk, P.A.Karplus. Structure-Based Insights Into the Role of the Cys-Tyr Crosslink and Inhibitor Recognition By Mammalian Cysteine Dioxygenase. J. Mol. Biol. V. 428 3999 2016.
ISSN: ESSN 1089-8638
PubMed: 27477048
DOI: 10.1016/J.JMB.2016.07.012