Chlorine in PDB 4yyo: Resting State of Rat Cysteine Dioxygenase C164S Variant

All present enzymatic activity of Resting State of Rat Cysteine Dioxygenase C164S Variant:
1.13.11.20;

The structure of Resting State of Rat Cysteine Dioxygenase C164S Variant, PDB code: 4yyo was solved by M.Fellner, E.P.Tchesnokov, E.Siakkou, M.T.Rutledge, 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)	21.09 / 1.77
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	57.800, 57.800, 123.070, 90.00, 90.00, 90.00
R / Rfree (%)	17.5 / 20.8

The structure of Resting State of Rat Cysteine Dioxygenase C164S Variant also contains other interesting chemical elements:

Iron

(Fe)

1 atom

The binding sites of Chlorine atom in the Resting State of Rat Cysteine Dioxygenase C164S Variant (pdb code 4yyo). 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 C164S Variant, PDB code: 4yyo:

Chlorine binding site 1 out of 1 in the Resting State of Rat Cysteine Dioxygenase C164S 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 C164S Variant within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl302 b:44.0 occ:1.00 FE A:FE2301 2.1 14.7 1.0 O A:HOH537 2.6 35.9 1.0 OH A:TYR157 2.6 25.1 1.0 NE2 A:HIS86 3.4 14.4 1.0 NE2 A:HIS88 3.6 14.2 1.0 CD2 A:LEU95 3.6 23.6 0.4 NE2 A:HIS140 3.6 15.8 1.0 ND1 A:HIS155 3.7 19.2 1.0 SG A:CYS93 3.7 20.4 1.0 CZ A:TYR157 3.8 26.3 1.0 CE1 A:HIS155 3.9 13.9 1.0 CE1 A:HIS86 4.1 14.1 1.0 CE1 A:HIS140 4.1 15.2 1.0 CD2 A:HIS88 4.2 17.6 1.0 CG A:LEU95 4.2 19.4 0.4 CE1 A:TYR157 4.3 21.5 1.0 CD2 A:HIS86 4.5 15.2 1.0 CD1 A:LEU95 4.5 15.9 0.6 CG2 A:VAL142 4.6 16.6 1.0 CE1 A:HIS88 4.7 16.6 1.0 CD1 A:LEU95 4.7 16.4 0.4 CD2 A:HIS140 4.8 14.9 1.0 CE2 A:TYR157 4.9 20.5 1.0

M.Fellner, E.Siakkou, A.S.Faponle, E.P.Tchesnokov, S.P.De Visser, S.M.Wilbanks, G.N.Jameson. Influence of Cysteine 164 on Active Site Structure in Rat Cysteine Dioxygenase. J.Biol.Inorg.Chem. V. 21 501 2016.
ISSN: ESSN 1432-1327
PubMed: 27193596
DOI: 10.1007/S00775-016-1360-0