Chlorine in PDB 5opc: Factor Inhibiting Hif (Fih) in Complex with Zinc and Vadadustat

All present enzymatic activity of Factor Inhibiting Hif (Fih) in Complex with Zinc and Vadadustat:
1.14.11.30;

The structure of Factor Inhibiting Hif (Fih) in Complex with Zinc and Vadadustat, PDB code: 5opc was solved by T.M.Leissing, C.J.Schofield, I.J.Clifton, X.Lu, D.Zhang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	75.07 / 2.30
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	86.799, 86.799, 149.520, 90.00, 90.00, 90.00
R / Rfree (%)	19.3 / 21.4

The structure of Factor Inhibiting Hif (Fih) in Complex with Zinc and Vadadustat also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Chlorine atom in the Factor Inhibiting Hif (Fih) in Complex with Zinc and Vadadustat (pdb code 5opc). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Factor Inhibiting Hif (Fih) in Complex with Zinc and Vadadustat, PDB code: 5opc:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Factor Inhibiting Hif (Fih) in Complex with Zinc and Vadadustat


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Factor Inhibiting Hif (Fih) in Complex with Zinc and Vadadustat within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl412 b:87.7 occ:0.16 CL A:A1Z412 0.0 87.7 0.2 C16 A:A1Z412 1.8 95.0 0.2 C15 A:A1Z412 2.8 94.3 0.2 C18 A:A1Z412 2.8 97.9 0.2 H151 A:A1Z412 2.8 0.1 0.2 H181 A:A1Z412 2.9 0.5 0.2 HH22 A:ARG238 2.9 0.3 1.0 C18 A:A1Z412 2.9 99.6 0.5 H181 A:A1Z412 3.0 0.5 0.5 NH2 A:ARG238 3.2 85.2 1.0 HH21 A:ARG238 3.2 0.3 1.0 C16 A:A1Z412 3.2 0.3 0.5 C19 A:A1Z412 3.3 95.3 0.5 H191 A:A1Z412 3.6 0.4 0.5 C15 A:A1Z412 3.8 97.4 0.5 C20 A:A1Z412 3.8 95.9 0.5 CL A:A1Z412 4.0 0.5 0.5 C14 A:A1Z412 4.0 96.7 0.2 C19 A:A1Z412 4.0 96.8 0.2 C14 A:A1Z412 4.1 95.7 0.5 CZ A:ARG238 4.1 72.7 1.0 O A:HOH558 4.3 68.6 1.0 H151 A:A1Z412 4.4 0.9 0.5 HH12 A:ARG238 4.4 81.2 1.0 H201 A:A1Z412 4.4 0.0 0.5 C20 A:A1Z412 4.6 93.7 0.2 NH1 A:ARG238 4.6 67.7 1.0 O A:HOH572 4.7 82.8 0.5 H191 A:A1Z412 4.8 0.1 0.2 HE A:ARG238 4.9 77.1 1.0 NE A:ARG238 4.9 64.2 1.0

Chlorine binding site 2 out of 2 in the Factor Inhibiting Hif (Fih) in Complex with Zinc and Vadadustat


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Factor Inhibiting Hif (Fih) in Complex with Zinc and Vadadustat within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl412 b:0.5 occ:0.50 CL A:A1Z412 0.0 0.5 0.5 C16 A:A1Z412 1.8 0.3 0.5 O A:HOH572 2.7 82.8 0.5 C18 A:A1Z412 2.7 97.9 0.2 C15 A:A1Z412 2.8 97.4 0.5 C18 A:A1Z412 2.8 99.6 0.5 H181 A:A1Z412 2.8 0.5 0.2 H151 A:A1Z412 2.8 0.9 0.5 H181 A:A1Z412 2.9 0.5 0.5 C19 A:A1Z412 3.1 96.8 0.2 C16 A:A1Z412 3.2 95.0 0.2 H191 A:A1Z412 3.3 0.1 0.2 C20 A:A1Z412 3.7 93.7 0.2 C15 A:A1Z412 3.8 94.3 0.2 CL A:A1Z412 4.0 87.7 0.2 OE1 A:GLN203 4.0 80.6 1.0 CD A:GLN203 4.0 75.5 1.0 C14 A:A1Z412 4.0 96.7 0.2 C14 A:A1Z412 4.0 95.7 0.5 C19 A:A1Z412 4.0 95.3 0.5 HG1 A:THR183 4.2 0.5 1.0 HG3 A:GLN203 4.2 82.0 1.0 NE2 A:GLN203 4.2 89.1 1.0 HE22 A:GLN203 4.2 1.0 1.0 H201 A:A1Z412 4.3 0.4 0.2 HB2 A:GLN203 4.4 74.3 1.0 HB3 A:TRP296 4.4 70.9 1.0 H151 A:A1Z412 4.4 0.1 0.2 CG A:TRP296 4.4 60.8 1.0 O A:HOH558 4.5 68.6 1.0 C20 A:A1Z412 4.6 95.9 0.5 HE21 A:GLN203 4.6 1.0 1.0 CG A:GLN203 4.6 68.3 1.0 CD1 A:TRP296 4.6 65.6 1.0 HG A:SER184 4.6 92.9 1.0 CD2 A:TRP296 4.6 65.8 1.0 HB2 A:TRP296 4.7 70.9 1.0 CB A:TRP296 4.8 59.1 1.0 H191 A:A1Z412 4.8 0.4 0.5 HB3 A:ASP201 4.8 58.9 1.0 OG1 A:THR183 4.8 92.1 1.0 HD1 A:TRP296 4.8 78.7 1.0 NE1 A:TRP296 4.9 62.6 1.0 CE2 A:TRP296 4.9 67.5 1.0 H121 A:A1Z412 4.9 0.1 1.0

T.L.Yeh, T.M.Leissing, M.I.Abboud, C.C.Thinnes, O.Atasoylu, J.P.Holt-Martyn, D.Zhang, A.Tumber, K.Lippl, C.T.Lohans, I.K.H.Leung, H.Morcrette, I.J.Clifton, T.D.W.Claridge, A.Kawamura, E.Flashman, X.Lu, P.J.Ratcliffe, R.Chowdhury, C.W.Pugh, C.J.Schofield. Molecular and Cellular Mechanisms of Hif Prolyl Hydroxylase Inhibitors in Clinical Trials. Chem Sci V. 8 7651 2017.
ISSN: ISSN 2041-6520
PubMed: 29435217
DOI: 10.1039/C7SC02103H