Iron in PDB 4piz: Homocysteine-Bound Cysteine Dioxygenase at pH 6.2

All present enzymatic activity of Homocysteine-Bound Cysteine Dioxygenase at pH 6.2:
1.13.11.20;

The structure of Homocysteine-Bound Cysteine Dioxygenase at pH 6.2, PDB code: 4piz 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 / 1.40
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 (%)	17.5 / 20.2

The binding sites of Iron atom in the Homocysteine-Bound Cysteine Dioxygenase at pH 6.2 (pdb code 4piz). 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 Homocysteine-Bound Cysteine Dioxygenase at pH 6.2, PDB code: 4piz:

Iron binding site 1 out of 1 in the Homocysteine-Bound Cysteine Dioxygenase at pH 6.2


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Homocysteine-Bound Cysteine Dioxygenase at pH 6.2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:17.0 occ:1.00 NE2 A:HIS86 2.0 18.2 1.0 NE2 A:HIS140 2.1 20.8 1.0 NE2 A:HIS88 2.1 17.8 1.0 SD A:HCS502 2.1 26.3 1.0 CE1 A:HIS88 3.0 18.5 1.0 CD2 A:HIS86 3.0 18.3 1.0 CE1 A:HIS86 3.0 18.6 1.0 CD2 A:HIS140 3.0 18.7 1.0 CG A:HCS502 3.0 45.3 1.0 CE1 A:HIS140 3.1 20.6 1.0 CD2 A:HIS88 3.2 17.6 1.0 N A:HCS502 3.4 46.9 1.0 CA A:HCS502 3.9 44.9 1.0 CB A:HCS502 4.0 41.9 1.0 ND1 A:HIS86 4.1 18.2 1.0 CG A:HIS86 4.1 17.8 1.0 ND1 A:HIS88 4.2 19.1 1.0 ND1 A:HIS140 4.2 18.4 1.0 CG A:HIS140 4.2 19.0 1.0 CG A:HIS88 4.3 20.7 1.0 OH A:TYR157 4.4 30.5 1.0 SG A:CYS93 4.4 23.0 1.0 O A:HOH765 4.5 29.9 1.0 CG2 A:ILE133 4.7 20.8 1.0 CG2 A:VAL142 4.7 21.8 1.0 CD2 A:LEU95 4.8 33.0 0.5

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