Atomistry » Iron » PDB 2xv1-2yde » 2y0i
Atomistry »
  Iron »
    PDB 2xv1-2yde »
      2y0i »

Iron in PDB 2y0i: Factor Inhibiting Hif-1 Alpha in Complex with Tankyrase-2 (TNKS2) Fragment Peptide (21-Mer)

Enzymatic activity of Factor Inhibiting Hif-1 Alpha in Complex with Tankyrase-2 (TNKS2) Fragment Peptide (21-Mer)

All present enzymatic activity of Factor Inhibiting Hif-1 Alpha in Complex with Tankyrase-2 (TNKS2) Fragment Peptide (21-Mer):
1.14.11.16; 2.4.2.30;

Protein crystallography data

The structure of Factor Inhibiting Hif-1 Alpha in Complex with Tankyrase-2 (TNKS2) Fragment Peptide (21-Mer), PDB code: 2y0i 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) 55.94 / 2.28
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 86.490, 86.490, 146.710, 90.00, 90.00, 90.00
R / Rfree (%) 23 / 24.8

Iron Binding Sites:

The binding sites of Iron atom in the Factor Inhibiting Hif-1 Alpha in Complex with Tankyrase-2 (TNKS2) Fragment Peptide (21-Mer) (pdb code 2y0i). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Factor Inhibiting Hif-1 Alpha in Complex with Tankyrase-2 (TNKS2) Fragment Peptide (21-Mer), PDB code: 2y0i:

Iron binding site 1 out of 1 in 2y0i

Go back to Iron Binding Sites List in 2y0i
Iron binding site 1 out of 1 in the Factor Inhibiting Hif-1 Alpha in Complex with Tankyrase-2 (TNKS2) Fragment Peptide (21-Mer)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Factor Inhibiting Hif-1 Alpha in Complex with Tankyrase-2 (TNKS2) Fragment Peptide (21-Mer) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1350

b:51.0
occ:1.00
 O2 A:AKG1351 1.9 46.2 1.0
OD2 A:ASP201 2.1 33.8 1.0
O5 A:AKG1351 2.1 39.1 1.0
O A:HOH2050 2.1 40.1 1.0
NE2 A:HIS199 2.3 39.7 1.0
NE2 A:HIS279 2.4 37.1 1.0
C1 A:AKG1351 2.6 39.8 1.0
C2 A:AKG1351 2.7 40.2 1.0
CG A:ASP201 3.1 35.1 1.0
CE1 A:HIS199 3.2 37.8 1.0
CD2 A:HIS199 3.3 37.5 1.0
CE1 A:HIS279 3.3 35.5 1.0
CD2 A:HIS279 3.3 35.8 1.0
OD1 A:ASP201 3.5 30.9 1.0
O1 A:AKG1351 3.9 38.6 1.0
O A:HOH2051 4.1 32.5 1.0
C3 A:AKG1351 4.2 38.6 1.0
CZ2 A:TRP296 4.2 45.6 1.0
ND1 A:HIS199 4.3 37.7 1.0
CG A:HIS199 4.4 38.3 1.0
CB A:ASP201 4.4 34.4 1.0
ND1 A:HIS279 4.4 37.9 1.0
CG A:HIS279 4.5 39.3 1.0
CD2 S:HIS553 4.5 72.9 1.0
CG S:HIS553 4.6 75.7 1.0
C4 A:AKG1351 4.8 38.7 1.0
CB S:HIS553 4.9 75.4 1.0
NE1 A:TRP296 5.0 42.8 1.0
NE2 S:HIS553 5.0 71.6 1.0

Reference:

M.Yang, R.Chowdhury, W.Ge, R.B.Hamed, M.A.Mcdonough, T.D.Claridge, B.M.Kessler, M.E.Cockman, P.J.Ratcliffe, C.J.Schofield. Factor-Inhibiting Hypoxia-Inducible Factor (Fih) Catalyses the Post-Translational Hydroxylation of Histidinyl Residues Within Ankyrin Repeat Domains. Febs J. V. 278 1086 2011.
ISSN: ISSN 1742-4658
PubMed: 21251231
DOI: 10.1111/J.1742-4658.2011.08022.X
Page generated: Sun Aug 4 05:04:10 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy