Iron 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:

Chlorine

(Cl)

1 atom

The binding sites of Iron 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 Iron atom.
In total only one binding site of Iron was determined in the D-Cysteine Bound C93A Mutant of Cysteine Dioxygenase at pH 8, PDB code: 5i0r:

Iron 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 Iron with other atoms in the Fe 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:Fe501 b:11.2 occ:1.00 H2 A:DCY502 1.7 15.7 0.5 H2 A:DCY502 1.8 17.5 0.1 N A:DCY502 2.0 13.1 0.5 NE2 A:HIS140 2.0 11.3 1.0 NE2 A:HIS88 2.0 12.1 1.0 N A:DCY502 2.1 14.6 0.1 NE2 A:HIS86 2.1 11.5 0.5 SG A:DCY502 2.2 16.7 0.5 CL A:CL503 2.3 15.0 0.5 HG A:DCY502 2.4 14.0 0.1 SG A:DCY502 2.6 11.7 0.1 H A:DCY502 2.7 15.7 0.5 H A:DCY502 2.8 17.5 0.1 CE1 A:HIS88 2.9 10.3 1.0 CE1 A:HIS140 3.0 10.8 1.0 CA A:DCY502 3.0 13.4 0.5 CA A:DCY502 3.0 8.4 0.1 CD2 A:HIS86 3.0 9.9 0.5 CD2 A:HIS140 3.1 10.6 1.0 HE1 A:HIS88 3.1 12.3 1.0 CD2 A:HIS88 3.1 12.0 1.0 HG A:DCY502 3.1 20.1 0.5 HD2 A:HIS86 3.1 11.9 0.5 CB A:DCY502 3.1 18.4 0.5 HE1 A:HIS140 3.1 12.9 1.0 CB A:DCY502 3.2 15.9 0.1 CE1 A:HIS86 3.2 9.9 0.5 HB2 A:DCY502 3.3 19.1 0.1 HA A:DCY502 3.3 10.0 0.1 HD2 A:HIS140 3.3 12.8 1.0 HA A:DCY502 3.3 16.1 0.5 HD2 A:HIS88 3.3 14.3 1.0 HB2 A:DCY502 3.4 22.1 0.5 HE1 A:HIS86 3.4 11.8 0.5 O A:HOH667 3.7 24.3 0.6 HH A:TYR157 3.9 18.6 1.0 HB3 A:DCY502 4.0 22.1 0.5 O A:HOH746 4.1 23.0 1.0 ND1 A:HIS88 4.1 11.1 1.0 HB3 A:DCY502 4.1 19.1 0.1 ND1 A:HIS140 4.1 12.1 1.0 HG21 A:ILE133 4.1 14.8 1.0 CG A:HIS140 4.2 11.0 1.0 CG A:HIS88 4.2 10.8 1.0 CG A:HIS86 4.2 10.6 0.5 HG21 A:VAL142 4.2 17.3 1.0 HB2 A:HIS86 4.3 17.1 0.6 ND1 A:HIS86 4.3 7.2 0.5 HE1 A:TYR157 4.3 17.9 1.0 HG23 A:VAL142 4.3 17.3 1.0 C A:DCY502 4.3 16.3 0.5 C A:DCY502 4.4 20.1 0.1 O A:DCY502 4.6 13.6 0.5 HB3 A:HIS86 4.7 17.1 0.6 HG22 A:ILE133 4.7 14.8 1.0 O A:DCY502 4.7 21.4 0.1 CG2 A:VAL142 4.7 14.4 1.0 OH A:TYR157 4.8 15.5 1.0 CG2 A:ILE133 4.8 12.4 1.0 HD12 A:LEU95 4.8 21.2 1.0 O A:HOH793 4.8 21.4 1.0 HD1 A:HIS88 4.9 13.3 1.0 O A:HOH685 4.9 28.0 1.0 HD1 A:HIS140 4.9 14.5 1.0 HG23 A:ILE133 4.9 14.8 1.0 CB A:HIS86 4.9 14.2 0.6

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