Chlorine in PDB 7q5x: Hif Prolyl Hydroxylase 2 (PHD2/EGLN1) in Complex with 2-Oxoglutarate (2OG) and Hif-2 Alpha Codd (523-542)

Enzymatic activity of Hif Prolyl Hydroxylase 2 (PHD2/EGLN1) in Complex with 2-Oxoglutarate (2OG) and Hif-2 Alpha Codd (523-542)

All present enzymatic activity of Hif Prolyl Hydroxylase 2 (PHD2/EGLN1) in Complex with 2-Oxoglutarate (2OG) and Hif-2 Alpha Codd (523-542):
1.14.11.29;

Protein crystallography data

The structure of Hif Prolyl Hydroxylase 2 (PHD2/EGLN1) in Complex with 2-Oxoglutarate (2OG) and Hif-2 Alpha Codd (523-542), PDB code: 7q5x was solved by W.D.Figg Jr, M.A.Mcdonough, R.Chowdhury, Y.Nakashima, C.J.Schofield, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.75 / 1.21
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 130.454, 38.175, 42.751, 90, 90, 90
R / Rfree (%) 15.7 / 17.6

Other elements in 7q5x:

The structure of Hif Prolyl Hydroxylase 2 (PHD2/EGLN1) in Complex with 2-Oxoglutarate (2OG) and Hif-2 Alpha Codd (523-542) also contains other interesting chemical elements:

Manganese (Mn) 1 atom
Magnesium (Mg) 3 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Hif Prolyl Hydroxylase 2 (PHD2/EGLN1) in Complex with 2-Oxoglutarate (2OG) and Hif-2 Alpha Codd (523-542) (pdb code 7q5x). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Hif Prolyl Hydroxylase 2 (PHD2/EGLN1) in Complex with 2-Oxoglutarate (2OG) and Hif-2 Alpha Codd (523-542), PDB code: 7q5x:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in 7q5x

Go back to Chlorine Binding Sites List in 7q5x
Chlorine binding site 1 out of 3 in the Hif Prolyl Hydroxylase 2 (PHD2/EGLN1) in Complex with 2-Oxoglutarate (2OG) and Hif-2 Alpha Codd (523-542)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Hif Prolyl Hydroxylase 2 (PHD2/EGLN1) in Complex with 2-Oxoglutarate (2OG) and Hif-2 Alpha Codd (523-542) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl518

b:51.6
occ:1.00
 HE1 A:TRP367 2.3 16.0 1.0
O A:HOH683 2.6 36.7 1.0
O A:HOH715 2.6 57.9 1.0
NE1 A:TRP367 3.2 13.3 1.0
O A:ASN203 3.2 21.1 1.0
O A:MET202 3.4 13.5 1.0
HH11 A:ARG371 3.7 23.6 1.0
H A:GLY206 3.7 15.6 1.0
HA3 A:GLY206 3.8 14.8 1.0
N A:GLY206 3.8 12.9 1.0
HA A:ASN203 3.8 17.4 1.0
C A:ASN203 3.9 16.1 1.0
HA2 A:GLY206 3.9 14.8 1.0
HD1 A:TRP367 3.9 16.4 1.0
CD1 A:TRP367 4.0 13.7 1.0
CA A:GLY206 4.0 12.3 1.0
C A:HIS205 4.2 13.1 1.0
NH1 A:ARG371 4.2 19.7 1.0
HZ2 A:TRP367 4.2 17.5 1.0
CE2 A:TRP367 4.3 12.0 1.0
O A:HOH709 4.3 41.3 1.0
C A:LYS204 4.3 14.9 1.0
HH12 A:ARG371 4.3 23.6 1.0
N A:HIS205 4.3 13.5 1.0
HD2 A:ARG371 4.3 20.1 1.0
CA A:ASN203 4.4 14.5 1.0
O A:LYS204 4.4 17.1 1.0
H A:HIS205 4.5 16.1 1.0
C A:MET202 4.5 12.2 1.0
N A:LYS204 4.5 14.2 1.0
O A:HOH720 4.5 35.9 1.0
CZ2 A:TRP367 4.6 14.6 1.0
CA A:HIS205 4.7 13.5 1.0
O A:HOH697 4.7 30.3 1.0
HA A:LYS204 4.7 18.2 1.0
CA A:LYS204 4.8 15.2 1.0
HA A:HIS205 4.8 16.2 1.0
O A:HIS205 4.8 13.7 1.0
O A:HOH649 4.9 15.5 1.0
N A:ASN203 5.0 12.8 1.0

Chlorine binding site 2 out of 3 in 7q5x

Go back to Chlorine Binding Sites List in 7q5x
Chlorine binding site 2 out of 3 in the Hif Prolyl Hydroxylase 2 (PHD2/EGLN1) in Complex with 2-Oxoglutarate (2OG) and Hif-2 Alpha Codd (523-542)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Hif Prolyl Hydroxylase 2 (PHD2/EGLN1) in Complex with 2-Oxoglutarate (2OG) and Hif-2 Alpha Codd (523-542) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl519

b:58.8
occ:1.00
 HH11 A:ARG312 2.0 24.7 1.0
HD2 A:ARG312 2.8 21.0 1.0
NH1 A:ARG312 2.8 20.6 1.0
HB2 A:PRO373 3.0 15.4 1.0
HG2 A:ARG312 3.0 20.1 1.0
HH12 A:ARG312 3.1 24.7 1.0
HB3 A:PRO373 3.3 15.4 1.0
HG2 A:PRO373 3.4 20.7 1.0
CB A:PRO373 3.5 12.8 1.0
CD A:ARG312 3.5 17.5 1.0
CG A:ARG312 3.6 16.7 1.0
HG3 A:ARG312 3.6 20.1 1.0
CG A:PRO373 3.8 17.2 1.0
O A:HOH726 3.8 37.6 1.0
CZ A:ARG312 3.9 18.8 1.0
HG3 A:PRO373 4.0 20.7 1.0
NE A:ARG312 4.2 20.1 1.0
HD3 A:ARG312 4.3 21.0 1.0
HB2 A:PHE346 4.6 16.8 1.0
CA A:PRO373 4.9 10.6 1.0
HD1 A:PHE346 5.0 18.9 1.0

Chlorine binding site 3 out of 3 in 7q5x

Go back to Chlorine Binding Sites List in 7q5x
Chlorine binding site 3 out of 3 in the Hif Prolyl Hydroxylase 2 (PHD2/EGLN1) in Complex with 2-Oxoglutarate (2OG) and Hif-2 Alpha Codd (523-542)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Hif Prolyl Hydroxylase 2 (PHD2/EGLN1) in Complex with 2-Oxoglutarate (2OG) and Hif-2 Alpha Codd (523-542) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl520

b:64.0
occ:1.00
 H A:ILE292 2.1 16.8 1.0
H A:GLY285 2.3 44.0 1.0
HB3 A:ASN284 2.7 82.8 1.0
CG A:ASN284 2.8 60.4 1.0
HA A:LYS291 2.8 20.6 1.0
HA A:ASN284 2.8 57.7 1.0
N A:GLY285 2.9 36.7 1.0
ND2 A:ASN284 2.9 58.5 1.0
HD22 A:ASN284 3.0 70.2 1.0
N A:ILE292 3.0 14.0 1.0
CB A:ASN284 3.0 69.0 1.0
CA A:ASN284 3.2 48.0 1.0
HD21 A:ASN284 3.3 70.2 1.0
OD1 A:ASN284 3.3 73.2 1.0
C A:ASN284 3.3 31.0 1.0
HB A:ILE292 3.4 20.3 1.0
O A:HOH636 3.6 26.3 1.0
CA A:LYS291 3.6 17.2 1.0
HG13 A:ILE292 3.7 23.0 1.0
HA2 A:GLY285 3.7 25.9 1.0
C A:LYS291 3.7 17.4 1.0
CA A:GLY285 3.9 21.6 1.0
O A:TYR290 3.9 22.1 1.0
HG3 A:LYS291 3.9 33.3 1.0
CA A:ILE292 3.9 16.1 1.0
HB2 A:ASN284 3.9 82.8 1.0
CB A:ILE292 4.0 16.9 1.0
O A:ILE292 4.0 20.4 1.0
CG1 A:ILE292 4.3 19.2 1.0
HA3 A:GLY285 4.3 25.9 1.0
HG2 A:LYS291 4.4 33.3 1.0
O A:ASN284 4.4 39.1 1.0
C A:ILE292 4.4 17.1 1.0
HD12 A:ILE292 4.4 23.7 1.0
CG A:LYS291 4.5 27.8 1.0
N A:LYS291 4.5 17.7 1.0
C A:TYR290 4.5 19.0 1.0
N A:ASN284 4.6 49.0 1.0
CB A:LYS291 4.6 18.9 1.0
HA A:ILE292 4.7 19.4 1.0
CD1 A:ILE292 4.9 19.8 1.0
O A:LYS291 4.9 18.3 1.0
H A:ASN284 5.0 58.8 1.0

Reference:

W.D.Figg Jr, M.A.Mcdonough, R.Chowdhury, Y.Nakashima, C.J.Schofield. Hif Prolyl Hydroxylase 2 (PHD2/EGLN1) in Complex with 2_OXOGLUTARATE (2OG) and Hif-2 Alpha Codd (523-542) To Be Published.
Page generated: Tue Apr 4 21:21:57 2023

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