Chlorine in PDB 4ubh: Resting State of Rat Cysteine Dioxygenase Y157F Variant

All present enzymatic activity of Resting State of Rat Cysteine Dioxygenase Y157F Variant:
1.13.11.20;

The structure of Resting State of Rat Cysteine Dioxygenase Y157F Variant, PDB code: 4ubh was solved by E.P.Tchesnokov, M.Fellner, G.N.L.Jameson, S.M.Wilbanks, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.84 / 1.81
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	57.790, 57.790, 121.990, 90.00, 90.00, 90.00
R / Rfree (%)	19 / 23.3

The structure of Resting State of Rat Cysteine Dioxygenase Y157F Variant also contains other interesting chemical elements:

Iron	(Fe)	1 atom
Sodium	(Na)	10 atoms

The binding sites of Chlorine atom in the Resting State of Rat Cysteine Dioxygenase Y157F Variant (pdb code 4ubh). 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 Resting State of Rat Cysteine Dioxygenase Y157F Variant, PDB code: 4ubh:

Chlorine binding site 1 out of 1 in the Resting State of Rat Cysteine Dioxygenase Y157F Variant


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Resting State of Rat Cysteine Dioxygenase Y157F Variant within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl311 b:15.4 occ:1.00 FE A:FE2301 2.2 7.1 1.0 ND1 A:HIS155 3.4 11.0 1.0 CE1 A:HIS155 3.4 8.1 1.0 O A:HOH578 3.5 18.1 1.0 NE2 A:HIS86 3.6 9.4 1.0 NE2 A:HIS88 3.6 4.8 1.0 NE2 A:HIS140 3.7 7.4 1.0 SG A:CYS93 3.8 14.4 1.0 CZ A:PHE157 3.9 13.5 1.0 CE1 A:PHE157 4.1 13.1 1.0 CE1 A:HIS86 4.1 7.9 1.0 CE1 A:HIS140 4.1 8.6 1.0 CD2 A:HIS88 4.3 8.9 1.0 CD1 A:LEU95 4.5 17.6 1.0 CG2 A:VAL142 4.7 7.8 1.0 CD2 A:HIS86 4.7 11.7 1.0 CG A:HIS155 4.7 8.6 1.0 CE1 A:HIS88 4.7 11.9 1.0 NE2 A:HIS155 4.7 8.7 1.0 CD2 A:HIS140 4.9 11.1 1.0

E.P.Tchesnokov, M.Fellner, G.N.L.Jameson, S.M.Wilbanks. Crystal Structure of Cysteine Dioxygenase Mutant To Be Published.