Chlorine in PDB 8q6e: Aerobic Crystal Structure of Hif Prolyl Hydroxylase 2 (PHD2 181-407) in Complex with Fe(III), 2-Oxoglutarate (2OG) and HIF2ALPHA-Codd Peptide

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

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

Protein crystallography data

The structure of Aerobic Crystal Structure of Hif Prolyl Hydroxylase 2 (PHD2 181-407) in Complex with Fe(III), 2-Oxoglutarate (2OG) and HIF2ALPHA-Codd Peptide, PDB code: 8q6e 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) 42.77 / 1.37
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 130.9, 38.12, 42.77, 90, 90, 90
R / Rfree (%) 18 / 20.5

Other elements in 8q6e:

The structure of Aerobic Crystal Structure of Hif Prolyl Hydroxylase 2 (PHD2 181-407) in Complex with Fe(III), 2-Oxoglutarate (2OG) and HIF2ALPHA-Codd Peptide also contains other interesting chemical elements:

Iron (Fe) 1 atom
Magnesium (Mg) 3 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Aerobic Crystal Structure of Hif Prolyl Hydroxylase 2 (PHD2 181-407) in Complex with Fe(III), 2-Oxoglutarate (2OG) and HIF2ALPHA-Codd Peptide (pdb code 8q6e). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Aerobic Crystal Structure of Hif Prolyl Hydroxylase 2 (PHD2 181-407) in Complex with Fe(III), 2-Oxoglutarate (2OG) and HIF2ALPHA-Codd Peptide, PDB code: 8q6e:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 8q6e

Go back to Chlorine Binding Sites List in 8q6e
Chlorine binding site 1 out of 2 in the Aerobic Crystal Structure of Hif Prolyl Hydroxylase 2 (PHD2 181-407) in Complex with Fe(III), 2-Oxoglutarate (2OG) and HIF2ALPHA-Codd Peptide


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Aerobic Crystal Structure of Hif Prolyl Hydroxylase 2 (PHD2 181-407) in Complex with Fe(III), 2-Oxoglutarate (2OG) and HIF2ALPHA-Codd Peptide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl504

b:23.6
occ:0.00
 HE1 A:TRP367 2.3 25.6 1.0
O A:HOH737 2.6 36.4 1.0
O A:HOH778 2.8 31.7 1.0
O A:ASN203 3.1 25.3 1.0
NE1 A:TRP367 3.2 21.3 1.0
O A:MET202 3.3 20.4 1.0
H A:GLY206 3.6 22.5 1.0
N A:GLY206 3.7 18.7 1.0
HA3 A:GLY206 3.7 21.7 1.0
HH11 A:ARG371 3.8 28.4 1.0
C A:ASN203 3.8 21.4 1.0
HA A:ASN203 3.8 23.8 1.0
HA2 A:GLY206 3.9 21.7 1.0
HD1 A:TRP367 3.9 25.1 1.0
CD1 A:TRP367 4.0 20.9 1.0
CA A:GLY206 4.0 18.1 1.0
HZ2 A:TRP367 4.1 25.9 1.0
C A:HIS205 4.1 20.7 1.0
N A:HIS205 4.2 19.1 1.0
CE2 A:TRP367 4.2 19.6 1.0
C A:LYS204 4.2 20.9 1.0
NH1 A:ARG371 4.3 23.6 1.0
HH12 A:ARG371 4.3 28.4 1.0
CA A:ASN203 4.3 19.8 1.0
HD2 A:ARG371 4.3 26.1 1.0
H A:HIS205 4.3 22.9 1.0
O A:LYS204 4.4 24.6 1.0
C A:MET202 4.5 20.5 1.0
O A:HOH771 4.5 34.9 1.0
O A:HOH704 4.5 30.5 1.0
O A:HOH815 4.6 39.4 1.0
N A:LYS204 4.6 20.0 1.0
CZ2 A:TRP367 4.6 21.5 1.0
CA A:HIS205 4.6 19.5 1.0
HA A:HIS205 4.7 23.4 1.0
HA A:LYS204 4.8 25.7 1.0
O A:HIS205 4.8 19.8 1.0
CA A:LYS204 4.8 21.4 1.0
N A:ASN203 5.0 19.8 1.0

Chlorine binding site 2 out of 2 in 8q6e

Go back to Chlorine Binding Sites List in 8q6e
Chlorine binding site 2 out of 2 in the Aerobic Crystal Structure of Hif Prolyl Hydroxylase 2 (PHD2 181-407) in Complex with Fe(III), 2-Oxoglutarate (2OG) and HIF2ALPHA-Codd Peptide


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Aerobic Crystal Structure of Hif Prolyl Hydroxylase 2 (PHD2 181-407) in Complex with Fe(III), 2-Oxoglutarate (2OG) and HIF2ALPHA-Codd Peptide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl505

b:28.4
occ:0.00
 H A:ILE292 2.0 22.9 1.0
O A:HOH739 2.3 40.5 1.0
H A:GLY285 2.4 36.9 1.0
O A:HOH766 2.6 40.6 1.0
HA A:ASN284 2.7 36.2 1.0
HA A:LYS291 2.8 27.5 1.0
N A:ILE292 2.8 19.1 1.0
O A:HOH638 3.1 31.2 1.0
N A:GLY285 3.1 30.7 1.0
HB A:ILE292 3.3 24.0 1.0
CA A:ASN284 3.5 30.2 1.0
CA A:LYS291 3.5 22.9 1.0
O A:HOH659 3.6 28.7 1.0
C A:LYS291 3.6 21.9 1.0
HG13 A:ILE292 3.7 25.7 1.0
C A:ASN284 3.8 24.9 1.0
CA A:ILE292 3.8 19.1 1.0
O A:ILE292 3.8 27.3 1.0
O A:TYR290 3.8 25.7 1.0
CB A:ILE292 3.9 20.0 1.0
CB A:ASN284 3.9 30.0 1.0
HA2 A:GLY285 3.9 30.1 1.0
CA A:GLY285 4.1 25.1 1.0
C A:ILE292 4.2 23.5 1.0
CG1 A:ILE292 4.3 21.4 1.0
N A:LYS291 4.4 23.5 1.0
C A:TYR290 4.4 23.3 1.0
HD12 A:ILE292 4.5 28.0 1.0
CB A:LYS291 4.6 29.3 1.0
HA3 A:GLY285 4.6 30.1 1.0
HA A:ILE292 4.6 22.9 1.0
N A:ASN284 4.6 29.0 1.0
O A:CYS283 4.7 27.6 1.0
O A:LYS291 4.8 25.6 1.0
CD1 A:ILE292 4.9 23.3 1.0
H A:LYS286 5.0 26.3 1.0
O A:HOH675 5.0 24.9 1.0
O A:ASN284 5.0 29.2 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 19:27:12 2024

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