Zinc in PDB 5jwp: Crystal Structure of Human Fih D201E Variant in Complex with Zn, Alpha-Ketoglutarate, and HIF1 Alpha Peptide.

Enzymatic activity of Crystal Structure of Human Fih D201E Variant in Complex with Zn, Alpha-Ketoglutarate, and HIF1 Alpha Peptide.

All present enzymatic activity of Crystal Structure of Human Fih D201E Variant in Complex with Zn, Alpha-Ketoglutarate, and HIF1 Alpha Peptide.:
1.14.11.30;

Protein crystallography data

The structure of Crystal Structure of Human Fih D201E Variant in Complex with Zn, Alpha-Ketoglutarate, and HIF1 Alpha Peptide., PDB code: 5jwp was solved by C.Y.Taabazuing, S.C.Garman, S.Eron, M.J.Knapp, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 34.37 / 2.10
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 86.220, 86.220, 149.903, 90.00, 90.00, 90.00
R / Rfree (%) 17 / 20.9

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Human Fih D201E Variant in Complex with Zn, Alpha-Ketoglutarate, and HIF1 Alpha Peptide. (pdb code 5jwp). 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 Crystal Structure of Human Fih D201E Variant in Complex with Zn, Alpha-Ketoglutarate, and HIF1 Alpha Peptide., PDB code: 5jwp:

Zinc binding site 1 out of 1 in 5jwp

Go back to Zinc Binding Sites List in 5jwp
Zinc binding site 1 out of 1 in the Crystal Structure of Human Fih D201E Variant in Complex with Zn, Alpha-Ketoglutarate, and HIF1 Alpha Peptide.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Human Fih D201E Variant in Complex with Zn, Alpha-Ketoglutarate, and HIF1 Alpha Peptide. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn403

b:37.5
occ:1.00
 OE1 A:GLU201 1.9 29.3 1.0
O2 A:AKG401 2.0 40.8 1.0
NE2 A:HIS279 2.1 37.1 1.0
NE2 A:HIS199 2.1 39.4 1.0
O5 A:AKG401 2.2 46.7 1.0
CD A:GLU201 2.7 33.5 1.0
C1 A:AKG401 2.8 43.7 1.0
C2 A:AKG401 2.8 45.4 1.0
CD2 A:HIS199 2.9 39.1 1.0
OE2 A:GLU201 2.9 34.8 1.0
CE1 A:HIS279 3.1 41.4 1.0
CD2 A:HIS279 3.1 40.7 1.0
CE1 A:HIS199 3.2 39.2 1.0
O A:HOH605 3.9 35.6 1.0
O1 A:AKG401 4.0 39.4 1.0
CG A:GLU201 4.1 34.3 1.0
CG A:HIS199 4.1 36.7 1.0
ND1 A:HIS279 4.2 41.6 1.0
CG A:HIS279 4.2 38.3 1.0
ND1 A:HIS199 4.2 36.5 1.0
C3 A:AKG401 4.4 46.7 1.0
CZ2 A:TRP296 4.4 41.3 1.0
CB A:GLU201 4.8 34.9 1.0
ND2 B:ASN803 4.8 38.3 1.0
CG B:ASN803 4.8 40.4 1.0
O B:HOH903 4.8 55.5 1.0
CB B:ASN803 4.9 41.1 1.0
ND2 A:ASN205 4.9 35.6 1.0

Reference:

J.A.Hangasky, C.Y.Taabazuing, C.B.Martin, S.J.Eron, M.J.Knapp. The Facial Triad in the Alpha-Ketoglutarate Dependent Oxygenase Fih: A Role For Sterics in Linking Substrate Binding to O2 Activation. J.Inorg.Biochem. V. 166 26 2016.
ISSN: ISSN 0162-0134
PubMed: 27815979
DOI: 10.1016/J.JINORGBIO.2016.10.007
Page generated: Wed Dec 16 06:25:58 2020

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