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Zinc in PDB 5op8: Factor Inhibiting Hif (Fih) in Complex with Zinc and Molidustat

Enzymatic activity of Factor Inhibiting Hif (Fih) in Complex with Zinc and Molidustat

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

Protein crystallography data

The structure of Factor Inhibiting Hif (Fih) in Complex with Zinc and Molidustat, PDB code: 5op8 was solved by T.M.Leissing, C.J.Schofield, I.J.Clifton, X.Lu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.39 / 2.30
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 86.180, 86.180, 148.200, 90.00, 90.00, 90.00
R / Rfree (%) 19.9 / 21.4

Zinc Binding Sites:

The binding sites of Zinc atom in the Factor Inhibiting Hif (Fih) in Complex with Zinc and Molidustat (pdb code 5op8). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Factor Inhibiting Hif (Fih) in Complex with Zinc and Molidustat, PDB code: 5op8:

Zinc binding site 1 out of 1 in 5op8

Go back to Zinc Binding Sites List in 5op8
Zinc binding site 1 out of 1 in the Factor Inhibiting Hif (Fih) in Complex with Zinc and Molidustat


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Factor Inhibiting Hif (Fih) in Complex with Zinc and Molidustat within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:50.5
occ:1.00
H101 A:A1H402 1.3 92.6 1.0
OD2 A:ASP201 2.0 42.5 1.0
N10 A:A1H402 2.0 77.1 1.0
NE2 A:HIS199 2.1 66.7 1.0
NE2 A:HIS279 2.1 53.8 1.0
N13 A:A1H402 2.6 82.1 1.0
CG A:ASP201 2.7 43.1 1.0
OD1 A:ASP201 2.8 45.4 1.0
N11 A:A1H402 2.9 75.8 1.0
CE1 A:HIS279 2.9 49.7 1.0
CD2 A:HIS199 3.0 48.7 1.0
HE1 A:HIS279 3.0 59.6 1.0
CE1 A:HIS199 3.0 54.2 1.0
C09 A:A1H402 3.1 58.3 1.0
C12 A:A1H402 3.2 86.9 1.0
HD2 A:HIS199 3.2 58.4 1.0
HE1 A:HIS199 3.2 65.1 1.0
CD2 A:HIS279 3.2 54.7 1.0
H091 A:A1H402 3.5 70.0 1.0
HD2 A:HIS279 3.5 65.7 1.0
HZ2 A:TRP296 3.7 85.4 1.0
C14 A:A1H402 3.7 0.4 1.0
H141 A:A1H402 3.9 0.1 1.0
O A:HOH530 4.0 51.5 1.0
ND1 A:HIS199 4.0 51.1 1.0
CG A:HIS199 4.1 46.7 1.0
C02 A:A1H402 4.1 78.9 1.0
ND1 A:HIS279 4.1 50.0 1.0
CB A:ASP201 4.2 39.5 1.0
C03 A:A1H402 4.2 70.6 1.0
CG A:HIS279 4.3 53.0 1.0
HB2 A:ASP201 4.4 47.4 1.0
HE1 A:TRP296 4.6 79.2 1.0
C23 A:A1H402 4.6 0.2 1.0
CZ2 A:TRP296 4.6 71.2 1.0
HB3 A:ASP201 4.7 47.4 1.0
HD1 A:HIS199 4.8 61.3 1.0
HD1 A:HIS279 4.8 60.0 1.0
N15 A:A1H402 4.9 0.8 1.0
HD22 A:ASN205 4.9 76.2 1.0
N A:ASP201 4.9 48.7 1.0
H32 A:GOL406 5.0 0.5 1.0

Reference:

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
Page generated: Sun Oct 27 23:45:39 2024

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