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Zinc in PDB 3d8c: Factor Inhibiting Hif-1 Alpha D201G Mutant in Complex with Zn(II), Alpha-Ketoglutarate and Hif-1 Alpha 19MER

Enzymatic activity of Factor Inhibiting Hif-1 Alpha D201G Mutant in Complex with Zn(II), Alpha-Ketoglutarate and Hif-1 Alpha 19MER

All present enzymatic activity of Factor Inhibiting Hif-1 Alpha D201G Mutant in Complex with Zn(II), Alpha-Ketoglutarate and Hif-1 Alpha 19MER:
1.14.11.16;

Protein crystallography data

The structure of Factor Inhibiting Hif-1 Alpha D201G Mutant in Complex with Zn(II), Alpha-Ketoglutarate and Hif-1 Alpha 19MER, PDB code: 3d8c was solved by M.A.Mcdonough, R.Chowdhury, C.J.Schofield, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.65 / 2.10
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 86.427, 86.427, 148.065, 90.00, 90.00, 90.00
R / Rfree (%) 21.8 / 25.6

Zinc Binding Sites:

The binding sites of Zinc atom in the Factor Inhibiting Hif-1 Alpha D201G Mutant in Complex with Zn(II), Alpha-Ketoglutarate and Hif-1 Alpha 19MER (pdb code 3d8c). 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 D201G Mutant in Complex with Zn(II), Alpha-Ketoglutarate and Hif-1 Alpha 19MER, PDB code: 3d8c:

Zinc binding site 1 out of 1 in 3d8c

Go back to Zinc Binding Sites List in 3d8c
Zinc binding site 1 out of 1 in the Factor Inhibiting Hif-1 Alpha D201G Mutant in Complex with Zn(II), Alpha-Ketoglutarate and Hif-1 Alpha 19MER


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 D201G Mutant in Complex with Zn(II), Alpha-Ketoglutarate and Hif-1 Alpha 19MER within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn350

b:37.1
occ:1.00
 NE2 A:HIS199 2.1 36.5 1.0
O2 A:AKG1351 2.2 48.3 1.0
O5 A:AKG1351 2.2 45.5 1.0
NE2 A:HIS279 2.3 36.2 1.0
O A:HOH1001 2.4 27.3 1.0
C1 A:AKG1351 2.9 45.9 1.0
C2 A:AKG1351 2.9 48.6 1.0
CE1 A:HIS199 3.1 33.6 1.0
CD2 A:HIS199 3.1 33.4 1.0
CD2 A:HIS279 3.1 37.4 1.0
CE1 A:HIS279 3.3 36.3 1.0
O A:HOH1040 3.9 39.5 1.0
O1 A:AKG1351 4.1 45.9 1.0
ND1 A:HIS199 4.1 34.9 1.0
CG A:HIS199 4.2 31.2 1.0
C3 A:AKG1351 4.2 46.3 1.0
CG A:HIS279 4.3 38.7 1.0
ND1 A:HIS279 4.4 38.0 1.0
CZ2 A:TRP296 4.4 40.6 1.0
CB B:ASN803 4.5 42.4 1.0
CG B:ASN803 4.6 41.9 1.0
ND2 B:ASN803 4.7 39.9 1.0
C4 A:AKG1351 4.9 43.4 1.0

Reference:

K.S.Hewitson, S.L.Holmes, D.Ehrismann, A.P.Hardy, R.Chowdhury, C.J.Schofield, M.A.Mcdonough. Evidence That Two Enzyme-Derived Histidine Ligands Are Sufficient For Iron Binding and Catalysis By Factor Inhibiting Hif (Fih). J.Biol.Chem. V. 283 25971 2008.
ISSN: ISSN 0021-9258
PubMed: 18611856
DOI: 10.1074/JBC.M804999200
Page generated: Thu Oct 24 12:06:04 2024

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