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Chlorine in PDB 9fdh: Closed Human Phosphoglycerate Kinase Complex with Bpg and Adp Produced By Cross-Soaking A Tsa Crystal

Enzymatic activity of Closed Human Phosphoglycerate Kinase Complex with Bpg and Adp Produced By Cross-Soaking A Tsa Crystal

All present enzymatic activity of Closed Human Phosphoglycerate Kinase Complex with Bpg and Adp Produced By Cross-Soaking A Tsa Crystal:
2.7.2.3;

Protein crystallography data

The structure of Closed Human Phosphoglycerate Kinase Complex with Bpg and Adp Produced By Cross-Soaking A Tsa Crystal, PDB code: 9fdh was solved by M.J.Cliff, J.P.Waltho, M.W.Bowler, N.J.Baxter, C.Bisson, G.M.Blackburn, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 70.07 / 1.76
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 38.845, 91.626, 108.734, 90, 90, 90
R / Rfree (%) 14.8 / 17.8

Other elements in 9fdh:

The structure of Closed Human Phosphoglycerate Kinase Complex with Bpg and Adp Produced By Cross-Soaking A Tsa Crystal also contains other interesting chemical elements:

Magnesium (Mg) 1 atom
Sodium (Na) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Closed Human Phosphoglycerate Kinase Complex with Bpg and Adp Produced By Cross-Soaking A Tsa Crystal (pdb code 9fdh). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Closed Human Phosphoglycerate Kinase Complex with Bpg and Adp Produced By Cross-Soaking A Tsa Crystal, PDB code: 9fdh:

Chlorine binding site 1 out of 1 in 9fdh

Go back to Chlorine Binding Sites List in 9fdh
Chlorine binding site 1 out of 1 in the Closed Human Phosphoglycerate Kinase Complex with Bpg and Adp Produced By Cross-Soaking A Tsa Crystal


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Closed Human Phosphoglycerate Kinase Complex with Bpg and Adp Produced By Cross-Soaking A Tsa Crystal within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl505

b:45.3
occ:1.00
 H A:ASP218 2.5 31.0 1.0
HH12 A:ARG65 2.6 37.7 1.0
O A:HOH771 2.8 52.2 1.0
HA A:LYS215 3.0 27.8 1.0
HB3 A:LYS215 3.0 27.7 1.0
HB3 A:ALA217 3.1 39.2 1.0
HB2 A:ASP218 3.2 37.8 1.0
OD2 A:ASP218 3.3 49.6 1.0
N A:ASP218 3.3 25.8 1.0
CG A:ASP218 3.3 46.6 1.0
NH1 A:ARG65 3.4 31.4 1.0
H A:ALA217 3.4 29.1 1.0
O A:HOH758 3.5 40.0 1.0
CA A:LYS215 3.5 23.2 1.0
C A:LYS215 3.5 26.6 1.0
HH22 A:ARG65 3.6 32.2 1.0
CB A:LYS215 3.6 23.0 1.0
HG2 A:LYS215 3.6 29.6 1.0
CB A:ASP218 3.7 31.5 1.0
O A:LYS215 3.8 24.9 1.0
OD1 A:ASP218 3.8 49.9 1.0
N A:ALA217 3.8 24.2 1.0
HH11 A:ARG65 3.9 37.7 1.0
CB A:ALA217 3.9 32.7 1.0
N A:VAL216 4.0 26.9 1.0
H A:VAL216 4.1 32.4 1.0
CA A:ASP218 4.1 25.6 1.0
CG A:LYS215 4.2 24.6 1.0
NH2 A:ARG65 4.2 26.8 1.0
CA A:ALA217 4.2 29.8 1.0
C A:ALA217 4.2 30.3 1.0
CZ A:ARG65 4.3 27.8 1.0
HB2 A:ALA217 4.4 39.2 1.0
HB2 A:LYS215 4.5 27.7 1.0
C A:VAL216 4.6 24.0 1.0
HB3 A:ASP218 4.6 37.8 1.0
HB1 A:ALA217 4.6 39.2 1.0
HD3 A:LYS215 4.6 28.2 1.0
HA A:ASP218 4.6 30.7 1.0
H A:LYS219 4.7 28.5 1.0
N A:LYS215 4.9 22.0 1.0
CA A:VAL216 4.9 23.9 1.0
HG3 A:LYS215 4.9 29.6 1.0
HH21 A:ARG65 5.0 32.2 1.0
O A:ALA214 5.0 26.9 1.0

Reference:

M.J.Cliff, Z.Serimbetov, C.Bisson, N.J.Baxter, G.M.Blackburn, S.Hay, M.W.Bowler, J.P.Waltho. The Role of Magnesium in Catalysis By Phosphoglycerate Kinase To Be Published.
Page generated: Sun Jul 13 16:43:55 2025

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