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Chlorine in PDB 2y3i: The Structure of the Fully Closed Conformation of Human Pgk in Complex with L-Adp, 3PG and the Tsa Aluminium Tetrafluoride

Enzymatic activity of The Structure of the Fully Closed Conformation of Human Pgk in Complex with L-Adp, 3PG and the Tsa Aluminium Tetrafluoride

All present enzymatic activity of The Structure of the Fully Closed Conformation of Human Pgk in Complex with L-Adp, 3PG and the Tsa Aluminium Tetrafluoride:
2.7.2.3;

Protein crystallography data

The structure of The Structure of the Fully Closed Conformation of Human Pgk in Complex with L-Adp, 3PG and the Tsa Aluminium Tetrafluoride, PDB code: 2y3i was solved by M.W.Bowler, L.Chaloin, C.Lionne, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 38.419, 103.877, 203.094, 90.00, 90.00, 90.00
R / Rfree (%) 26.3 / 30.3

Other elements in 2y3i:

The structure of The Structure of the Fully Closed Conformation of Human Pgk in Complex with L-Adp, 3PG and the Tsa Aluminium Tetrafluoride also contains other interesting chemical elements:

Aluminium (Al) 2 atoms
Magnesium (Mg) 2 atoms
Fluorine (F) 8 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the The Structure of the Fully Closed Conformation of Human Pgk in Complex with L-Adp, 3PG and the Tsa Aluminium Tetrafluoride (pdb code 2y3i). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the The Structure of the Fully Closed Conformation of Human Pgk in Complex with L-Adp, 3PG and the Tsa Aluminium Tetrafluoride, PDB code: 2y3i:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 2y3i

Go back to Chlorine Binding Sites List in 2y3i
Chlorine binding site 1 out of 2 in the The Structure of the Fully Closed Conformation of Human Pgk in Complex with L-Adp, 3PG and the Tsa Aluminium Tetrafluoride


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of The Structure of the Fully Closed Conformation of Human Pgk in Complex with L-Adp, 3PG and the Tsa Aluminium Tetrafluoride within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1417

b:36.7
occ:1.00
N A:ASP218 3.1 30.3 1.0
C A:LYS215 3.3 29.7 1.0
CA A:LYS215 3.4 29.3 1.0
CB A:LYS215 3.4 29.1 1.0
N A:ALA217 3.5 30.8 1.0
CG A:ASP218 3.5 30.4 1.0
O A:LYS215 3.5 29.8 1.0
CB A:ASP218 3.5 29.8 1.0
N A:VAL216 3.7 30.1 1.0
OD1 A:ASP218 3.7 31.2 1.0
CB A:ALA217 3.8 31.3 1.0
NH1 A:ARG65 3.8 44.0 1.0
OD2 A:ASP218 3.9 30.2 1.0
CA A:ALA217 3.9 31.2 1.0
CA A:ASP218 4.0 30.0 1.0
C A:ALA217 4.0 30.8 1.0
C A:VAL216 4.2 30.4 1.0
CG A:LYS215 4.2 29.0 1.0
NH2 A:ARG65 4.3 39.9 1.0
CZ A:ARG65 4.5 41.4 1.0
CA A:VAL216 4.6 30.3 1.0
CD A:LYS215 4.7 29.0 1.0
N A:LYS215 4.8 29.0 1.0
O A:VAL216 4.9 30.6 1.0

Chlorine binding site 2 out of 2 in 2y3i

Go back to Chlorine Binding Sites List in 2y3i
Chlorine binding site 2 out of 2 in the The Structure of the Fully Closed Conformation of Human Pgk in Complex with L-Adp, 3PG and the Tsa Aluminium Tetrafluoride


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of The Structure of the Fully Closed Conformation of Human Pgk in Complex with L-Adp, 3PG and the Tsa Aluminium Tetrafluoride within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cl1419

b:36.7
occ:1.00
NH1 D:ARG65 3.4 27.8 1.0
CG D:ASP218 3.5 34.5 1.0
CB D:LYS215 3.5 28.2 1.0
N D:ASP218 3.5 33.4 1.0
CA D:LYS215 3.5 28.6 1.0
C D:LYS215 3.6 29.1 1.0
OD2 D:ASP218 3.7 33.9 1.0
CB D:ASP218 3.7 34.1 1.0
OD1 D:ASP218 3.7 35.7 1.0
O D:LYS215 3.9 29.3 1.0
N D:ALA217 3.9 31.9 1.0
NH2 D:ARG65 3.9 27.6 1.0
CB D:ALA217 4.0 31.7 1.0
N D:VAL216 4.1 29.4 1.0
CZ D:ARG65 4.1 27.5 1.0
CG D:LYS215 4.1 27.2 1.0
CA D:ASP218 4.2 33.7 1.0
CA D:ALA217 4.3 32.3 1.0
C D:ALA217 4.4 32.8 1.0
CD D:LYS215 4.5 26.7 1.0
C D:VAL216 4.6 31.0 1.0
N D:LYS215 4.9 27.7 1.0
CA D:VAL216 5.0 30.5 1.0

Reference:

P.Lallemand, L.Chaloin, B.Roy, T.Barman, M.W.Bowler, C.Lionne. Interaction of Human 3-Phosphoglycerate Kinase with Its Two Substrates: Is Substrate Antagonism A Kinetic Advantage? J.Mol.Biol. V. 409 742 2011.
ISSN: ISSN 0022-2836
PubMed: 21549713
DOI: 10.1016/J.JMB.2011.04.048
Page generated: Sat Jul 20 14:41:23 2024

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