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Zinc in PDB 2xum: Factor Inhibiting Hif (Fih) Q239H Mutant in Complex with Zn(II), Nog and Asp-Substrate Peptide (20-Mer)

Enzymatic activity of Factor Inhibiting Hif (Fih) Q239H Mutant in Complex with Zn(II), Nog and Asp-Substrate Peptide (20-Mer)

All present enzymatic activity of Factor Inhibiting Hif (Fih) Q239H Mutant in Complex with Zn(II), Nog and Asp-Substrate Peptide (20-Mer):
1.14.11.16;

Protein crystallography data

The structure of Factor Inhibiting Hif (Fih) Q239H Mutant in Complex with Zn(II), Nog and Asp-Substrate Peptide (20-Mer), PDB code: 2xum was solved by R.Chowdhury, M.A.Mcdonough, C.J.Schofield, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 74.12 / 2.20
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 86.352, 86.352, 144.533, 90.00, 90.00, 90.00
R / Rfree (%) 20.1 / 22.2

Zinc Binding Sites:

The binding sites of Zinc atom in the Factor Inhibiting Hif (Fih) Q239H Mutant in Complex with Zn(II), Nog and Asp-Substrate Peptide (20-Mer) (pdb code 2xum). 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) Q239H Mutant in Complex with Zn(II), Nog and Asp-Substrate Peptide (20-Mer), PDB code: 2xum:

Zinc binding site 1 out of 1 in 2xum

Go back to Zinc Binding Sites List in 2xum
Zinc binding site 1 out of 1 in the Factor Inhibiting Hif (Fih) Q239H Mutant in Complex with Zn(II), Nog and Asp-Substrate Peptide (20-Mer)


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) Q239H Mutant in Complex with Zn(II), Nog and Asp-Substrate Peptide (20-Mer) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn501

b:44.6
occ:1.00
OD2 A:ASP201 2.0 43.0 1.0
O2' A:OGA601 2.0 46.8 1.0
O1 A:OGA601 2.2 46.1 1.0
NE2 A:HIS199 2.2 48.2 1.0
O A:HOH2144 2.2 35.2 0.5
NE2 A:HIS279 2.3 48.1 1.0
C2 A:OGA601 2.8 46.0 1.0
C1 A:OGA601 2.9 45.0 1.0
CG A:ASP201 3.0 47.3 1.0
CE1 A:HIS199 3.1 46.8 1.0
CD2 A:HIS279 3.2 48.2 1.0
CD2 A:HIS199 3.2 45.5 1.0
OD1 A:ASP201 3.3 47.6 1.0
CE1 A:HIS279 3.3 46.6 1.0
O A:HOH2066 3.9 43.5 1.0
O2 A:OGA601 4.1 47.4 1.0
N1 A:OGA601 4.1 44.3 1.0
ND1 A:HIS199 4.2 45.0 1.0
CZ2 A:TRP296 4.3 51.9 1.0
CG A:HIS199 4.3 46.4 1.0
CG A:HIS279 4.3 48.4 1.0
ND1 A:HIS279 4.4 48.0 1.0
CB A:ASP201 4.4 47.0 1.0
O A:HOH2145 4.5 51.5 0.5
OD2 S:ASP803 4.9 39.3 1.0
C4 A:OGA601 4.9 44.1 1.0
ND2 A:ASN205 5.0 47.1 1.0

Reference:

M.Yang, W.Ge, R.Chowdhury, T.D.Claridge, H.B.Kramer, B.Schmierer, M.A.Mcdonough, L.Gong, B.M.Kessler, P.J.Ratcliffe, M.L.Coleman, C.J.Schofield. Asparagine and Aspartate Hydroxylation of the Cytoskeletal Ankyrin Family Is Catalyzed By Factor-Inhibiting Hypoxia-Inducible Factor. J. Biol. Chem. V. 286 7648 2011.
ISSN: ESSN 1083-351X
PubMed: 21177872
DOI: 10.1074/JBC.M110.193540
Page generated: Wed Dec 16 04:00:38 2020

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