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Zinc in PDB 4jaa: Factor Inhibiting Hif-1 Alpha in Complex with Consensus Ankyrin Repeat Domain-(D)Leu Peptide

Enzymatic activity of Factor Inhibiting Hif-1 Alpha in Complex with Consensus Ankyrin Repeat Domain-(D)Leu Peptide

All present enzymatic activity of Factor Inhibiting Hif-1 Alpha in Complex with Consensus Ankyrin Repeat Domain-(D)Leu Peptide:
1.14.11.30;

Protein crystallography data

The structure of Factor Inhibiting Hif-1 Alpha in Complex with Consensus Ankyrin Repeat Domain-(D)Leu Peptide, PDB code: 4jaa was solved by J.S.Scotti, W.Ge, 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) 33.80 / 2.39
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 86.079, 86.079, 147.029, 90.00, 90.00, 90.00
R / Rfree (%) 18.4 / 21.9

Zinc Binding Sites:

The binding sites of Zinc atom in the Factor Inhibiting Hif-1 Alpha in Complex with Consensus Ankyrin Repeat Domain-(D)Leu Peptide (pdb code 4jaa). 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-1 Alpha in Complex with Consensus Ankyrin Repeat Domain-(D)Leu Peptide, PDB code: 4jaa:

Zinc binding site 1 out of 1 in 4jaa

Go back to Zinc Binding Sites List in 4jaa
Zinc binding site 1 out of 1 in the Factor Inhibiting Hif-1 Alpha in Complex with Consensus Ankyrin Repeat Domain-(D)Leu Peptide


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-1 Alpha in Complex with Consensus Ankyrin Repeat Domain-(D)Leu Peptide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn501

b:21.4
occ:1.00
 OD2 A:ASP201 2.0 21.1 1.0
O2' A:OGA502 2.1 24.0 1.0
NE2 A:HIS279 2.1 21.7 1.0
NE2 A:HIS199 2.1 24.9 1.0
O1 A:OGA502 2.2 29.1 1.0
C2 A:OGA502 2.7 25.2 1.0
C1 A:OGA502 2.8 27.7 1.0
CE1 A:HIS199 2.8 24.6 1.0
CG A:ASP201 3.0 21.7 1.0
CE1 A:HIS279 3.0 21.4 1.0
CD2 A:HIS279 3.1 21.1 1.0
CD2 A:HIS199 3.2 25.2 1.0
OD1 A:ASP201 3.3 22.4 1.0
O A:HOH614 4.0 13.8 1.0
ND1 A:HIS199 4.0 25.3 1.0
O2 A:OGA502 4.0 26.9 1.0
ND1 A:HIS279 4.1 20.9 1.0
N1 A:OGA502 4.1 25.2 1.0
CB S:DLE803 4.2 35.9 1.0
CG A:HIS199 4.2 25.3 1.0
CG A:HIS279 4.2 20.8 1.0
CB A:ASP201 4.4 22.3 1.0
CD1 S:DLE803 4.5 38.3 1.0
CZ2 A:TRP296 4.5 26.9 1.0
CG S:DLE803 4.8 37.5 1.0
C4 A:OGA502 4.9 25.0 1.0
ND2 A:ASN205 5.0 23.1 1.0

Reference:

J.S.Scotti, W.Ge, M.A.Mcdonough, C.J.Schofield. Structure of An Oxygenase in Complex with Substrate To Be Published.
Page generated: Sun Oct 27 01:06:25 2024

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