Chlorine in PDB 5i0r: D-Cysteine Bound C93A Mutant of Cysteine Dioxygenase at pH 8

All present enzymatic activity of D-Cysteine Bound C93A Mutant of Cysteine Dioxygenase at pH 8:
1.13.11.20;

The structure of D-Cysteine Bound C93A Mutant of Cysteine Dioxygenase at pH 8, PDB code: 5i0r was solved by K.M.Kean, 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)	41.94 / 1.35
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 (%)	17 / 20

The structure of D-Cysteine Bound C93A Mutant of Cysteine Dioxygenase at pH 8 also contains other interesting chemical elements:

Iron

(Fe)

1 atom

The binding sites of Chlorine atom in the D-Cysteine Bound C93A Mutant of Cysteine Dioxygenase at pH 8 (pdb code 5i0r). 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 D-Cysteine Bound C93A Mutant of Cysteine Dioxygenase at pH 8, PDB code: 5i0r:

Chlorine binding site 1 out of 1 in the D-Cysteine Bound C93A Mutant of Cysteine Dioxygenase at pH 8


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of D-Cysteine Bound C93A Mutant of Cysteine Dioxygenase at pH 8 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl503 b:15.0 occ:0.45 SG A:DCY502 0.6 16.7 0.5 HG A:DCY502 1.2 20.1 0.5 HB2 A:DCY502 1.7 19.1 0.1 HG A:DCY502 1.8 14.0 0.1 FE A:FE501 2.3 11.2 1.0 CB A:DCY502 2.3 15.9 0.1 CB A:DCY502 2.3 18.4 0.5 SG A:DCY502 2.4 11.7 0.1 HH A:TYR157 2.4 18.6 1.0 HB3 A:DCY502 2.7 22.1 0.5 HB2 A:DCY502 2.9 22.1 0.5 O A:HOH685 3.0 28.0 1.0 CA A:DCY502 3.0 8.4 0.1 CA A:DCY502 3.1 13.4 0.5 H2 A:DCY502 3.1 15.7 0.5 HA A:DCY502 3.1 10.0 0.1 HB3 A:DCY502 3.1 19.1 0.1 HA A:DCY502 3.1 16.1 0.5 H2 A:DCY502 3.1 17.5 0.1 N A:DCY502 3.2 13.1 0.5 N A:DCY502 3.2 14.6 0.1 HE1 A:HIS155 3.2 11.8 1.0 OH A:TYR157 3.2 15.5 1.0 HE1 A:TYR157 3.3 17.9 1.0 ND1 A:HIS155 3.3 11.2 1.0 HD12 A:LEU95 3.4 21.2 1.0 HE1 A:HIS140 3.4 12.9 1.0 CE1 A:HIS155 3.6 9.8 1.0 NE2 A:HIS140 3.6 11.3 1.0 NE2 A:HIS88 3.6 12.1 1.0 CE1 A:HIS140 3.8 10.8 1.0 HD2 A:HIS88 3.9 14.3 1.0 O A:HOH793 4.0 21.4 1.0 CE1 A:TYR157 4.0 14.9 1.0 H A:DCY502 4.0 17.5 0.1 H A:DCY502 4.0 15.7 0.5 CZ A:TYR157 4.0 15.4 1.0 NE2 A:HIS86 4.1 11.5 0.5 HG21 A:VAL142 4.1 17.3 1.0 CD2 A:HIS88 4.1 12.0 1.0 HB2 A:LEU95 4.2 18.3 1.0 CD1 A:LEU95 4.3 17.7 1.0 C A:DCY502 4.4 16.3 0.5 C A:DCY502 4.5 20.1 0.1 CG A:HIS155 4.6 9.7 1.0 HD11 A:LEU95 4.6 21.2 1.0 CE1 A:HIS88 4.7 10.3 1.0 HB3 A:HIS155 4.8 12.6 1.0 HG A:LEU95 4.8 24.3 1.0 CB A:ALA93 4.8 10.7 1.0 HE1 A:HIS86 4.8 11.8 0.5 HD13 A:LEU95 4.9 21.2 1.0 NE2 A:HIS155 4.9 10.5 1.0 CE1 A:HIS86 4.9 9.9 0.5 CD2 A:HIS140 4.9 10.6 1.0 O A:HOH601 5.0 22.4 1.0 CG2 A:VAL142 5.0 14.4 1.0 HD22 A:LEU75 5.0 14.0 1.0 HG23 A:VAL142 5.0 17.3 1.0 HG22 A:ILE133 5.0 14.8 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