Atomistry » Iron » PDB 8py5-8qbc » 8q6d
Atomistry »
  Iron »
    PDB 8py5-8qbc »
      8q6d »

Iron in PDB 8q6d: Anaerobic Crystal Structure of Hif Prolyl Hydroxylase 2 (PHD2 181-407) in Complex with HIF2ALPHA-Codd Peptide (523-542), Fe(II) and 2- Oxoglutarate (2OG)

Enzymatic activity of Anaerobic Crystal Structure of Hif Prolyl Hydroxylase 2 (PHD2 181-407) in Complex with HIF2ALPHA-Codd Peptide (523-542), Fe(II) and 2- Oxoglutarate (2OG)

All present enzymatic activity of Anaerobic Crystal Structure of Hif Prolyl Hydroxylase 2 (PHD2 181-407) in Complex with HIF2ALPHA-Codd Peptide (523-542), Fe(II) and 2- Oxoglutarate (2OG):
1.14.11.29;

Protein crystallography data

The structure of Anaerobic Crystal Structure of Hif Prolyl Hydroxylase 2 (PHD2 181-407) in Complex with HIF2ALPHA-Codd Peptide (523-542), Fe(II) and 2- Oxoglutarate (2OG), PDB code: 8q6d was solved by G.Fiorini, W.D.Figg Jr, C.J.Schofield, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.55 / 1.40
Space group P 21 2 21
Cell size a, b, c (Å), α, β, γ (°) 38.07, 42.63, 130.75, 90, 90, 90
R / Rfree (%) 16.7 / 19

Iron Binding Sites:

The binding sites of Iron atom in the Anaerobic Crystal Structure of Hif Prolyl Hydroxylase 2 (PHD2 181-407) in Complex with HIF2ALPHA-Codd Peptide (523-542), Fe(II) and 2- Oxoglutarate (2OG) (pdb code 8q6d). 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 Anaerobic Crystal Structure of Hif Prolyl Hydroxylase 2 (PHD2 181-407) in Complex with HIF2ALPHA-Codd Peptide (523-542), Fe(II) and 2- Oxoglutarate (2OG), PDB code: 8q6d:

Iron binding site 1 out of 1 in 8q6d

Go back to Iron Binding Sites List in 8q6d
Iron binding site 1 out of 1 in the Anaerobic Crystal Structure of Hif Prolyl Hydroxylase 2 (PHD2 181-407) in Complex with HIF2ALPHA-Codd Peptide (523-542), Fe(II) and 2- Oxoglutarate (2OG)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Anaerobic Crystal Structure of Hif Prolyl Hydroxylase 2 (PHD2 181-407) in Complex with HIF2ALPHA-Codd Peptide (523-542), Fe(II) and 2- Oxoglutarate (2OG) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:13.7
occ:1.00
 O2 A:AKG502 2.1 14.8 1.0
OD1 A:ASP315 2.1 14.5 1.0
NE2 A:HIS374 2.1 14.7 1.0
NE2 A:HIS313 2.2 14.3 1.0
O A:HOH622 2.2 14.8 1.0
O5 A:AKG502 2.2 14.0 1.0
C2 A:AKG502 2.9 13.0 1.0
C1 A:AKG502 2.9 14.6 1.0
CE1 A:HIS313 3.1 14.9 1.0
CE1 A:HIS374 3.1 14.2 1.0
CG A:ASP315 3.1 13.9 1.0
CD2 A:HIS374 3.2 14.4 1.0
HE1 A:HIS313 3.2 17.9 1.0
HE1 A:HIS374 3.2 17.0 1.0
CD2 A:HIS313 3.3 14.1 1.0
HG3 B:PRO531 3.3 16.7 1.0
HD2 A:HIS374 3.4 17.3 1.0
OD2 A:ASP315 3.4 13.9 1.0
HD2 A:HIS313 3.5 16.9 1.0
HZ A:PHE366 3.9 17.6 1.0
HD3 B:PRO531 4.0 18.0 1.0
O1 A:AKG502 4.1 15.2 1.0
HZ2 A:TRP389 4.1 18.4 1.0
ND1 A:HIS374 4.2 14.1 1.0
O A:HOH676 4.2 14.8 1.0
ND1 A:HIS313 4.2 15.2 1.0
CG B:PRO531 4.2 13.9 1.0
CG A:HIS374 4.3 15.0 1.0
HA A:ASP315 4.3 15.6 1.0
C3 A:AKG502 4.3 15.0 1.0
CG A:HIS313 4.3 13.7 1.0
CB A:ASP315 4.5 13.8 1.0
H41 A:AKG502 4.5 18.2 1.0
CD B:PRO531 4.6 15.0 1.0
HE2 A:TYR310 4.6 17.8 1.0
H42 A:AKG502 4.7 18.2 1.0
H32 A:AKG502 4.7 18.0 1.0
CE2 A:TYR310 4.8 14.8 1.0
HG2 B:PRO531 4.8 16.7 1.0
C4 A:AKG502 4.8 15.2 1.0
HD2 B:PRO531 4.8 18.0 1.0
HG21 A:THR325 4.8 17.2 1.0
CA A:ASP315 4.8 13.0 1.0
CZ A:PHE366 4.8 14.6 1.0
HB3 B:PRO531 4.9 18.1 1.0
H31 A:AKG502 4.9 18.0 1.0
HE1 A:PHE366 4.9 18.1 1.0
HE1 A:TRP389 4.9 17.9 1.0
HD1 A:HIS374 5.0 17.0 1.0
HD1 A:HIS313 5.0 18.2 1.0
HB2 A:ASP315 5.0 16.5 1.0
N A:ASP315 5.0 13.2 1.0
H A:ASP315 5.0 15.9 1.0
HB3 A:ASP315 5.0 16.5 1.0

Reference:

G.Fiorini, W.D.Figg Jr, C.J.Schofield. Hif Prolyl Hydroxylase 2 in Complex with HIF2ALPHA-Codd To Be Published.
Page generated: Sat Sep 28 21:39:09 2024

Last articles

Zn in 9MJ5
Zn in 9HNW
Zn in 9G0L
Zn in 9FNE
Zn in 9DZN
Zn in 9E0I
Zn in 9D32
Zn in 9DAK
Zn in 8ZXC
Zn in 8ZUF
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy