Atomistry » Aluminium » PDB 2xzl-3wgu » 2y3i
Atomistry »
  Aluminium »
    PDB 2xzl-3wgu »
      2y3i »

Aluminium 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:

Magnesium (Mg) 2 atoms
Fluorine (F) 8 atoms
Chlorine (Cl) 2 atoms

Aluminium Binding Sites:

The binding sites of Aluminium 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 Aluminium atom.
In total 2 binding sites of Aluminium 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 Aluminium binding site number: 1; 2;

Aluminium binding site 1 out of 2 in 2y3i

Go back to Aluminium Binding Sites List in 2y3i
Aluminium 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 Aluminium with other atoms in the Al 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:Al1419

b:28.5
occ:1.00
AL A:ALF1419 0.0 28.5 1.0
F2 A:ALF1419 1.8 29.3 1.0
F1 A:ALF1419 1.8 28.2 1.0
F4 A:ALF1419 1.8 29.1 1.0
F3 A:ALF1419 1.8 30.4 1.0
O2 A:3PG1420 2.2 31.9 1.0
O1B A:LA81418 2.3 27.7 1.0
O3B A:LA81418 2.8 27.1 1.0
PB A:LA81418 3.1 27.1 1.0
C1 A:3PG1420 3.2 30.7 1.0
NZ A:LYS215 3.3 28.7 1.0
O1 A:3PG1420 3.5 31.0 1.0
MG A:MG1416 3.5 20.9 1.0
O1A A:LA81418 3.7 27.0 1.0
O2B A:LA81418 4.1 25.9 1.0
N A:GLY373 4.3 24.7 1.0
O3A A:LA81418 4.3 27.0 1.0
NH2 A:ARG38 4.3 33.5 1.0
NZ A:LYS219 4.4 27.3 1.0
CE A:LYS215 4.4 28.9 1.0
N A:GLY396 4.5 31.1 1.0
C2 A:3PG1420 4.5 29.9 1.0
PA A:LA81418 4.6 26.6 1.0
CA A:GLY372 4.8 25.4 1.0
N A:GLY395 4.8 30.5 1.0
O4P A:3PG1420 4.8 29.2 1.0
CA A:GLY395 4.8 30.6 1.0
OD1 A:ASP374 5.0 25.7 1.0

Aluminium binding site 2 out of 2 in 2y3i

Go back to Aluminium Binding Sites List in 2y3i
Aluminium 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 Aluminium with other atoms in the Al 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:Al1417

b:30.6
occ:1.00
AL D:ALF1417 0.0 30.6 1.0
F4 D:ALF1417 1.8 30.2 1.0
F1 D:ALF1417 1.8 31.0 1.0
F3 D:ALF1417 1.8 32.4 1.0
F2 D:ALF1417 1.8 31.2 1.0
O1B D:LA81416 2.0 27.2 1.0
O2 D:3PG1420 2.3 32.8 1.0
PB D:LA81416 3.2 27.1 1.0
C1 D:3PG1420 3.2 32.5 1.0
O3B D:LA81416 3.2 26.8 1.0
O1 D:3PG1420 3.4 33.0 1.0
NZ D:LYS215 3.5 27.0 1.0
MG D:MG1418 3.6 18.2 1.0
O1A D:LA81416 3.7 29.4 1.0
O D:HOH2005 4.1 21.2 1.0
O2B D:LA81416 4.2 27.3 1.0
N D:GLY396 4.2 34.5 1.0
O3A D:LA81416 4.3 27.7 1.0
N D:GLY373 4.4 31.8 1.0
NH2 D:ARG38 4.4 34.3 1.0
NZ D:LYS219 4.4 33.8 1.0
N D:GLY395 4.5 34.0 1.0
CE D:LYS215 4.6 26.5 1.0
C2 D:3PG1420 4.6 32.2 1.0
PA D:LA81416 4.6 29.2 1.0
CA D:GLY395 4.6 34.3 1.0
CA D:GLY372 4.7 32.1 1.0
OD1 D:ASN336 4.8 33.0 1.0
C D:GLY395 4.9 34.1 1.0
C3 D:3PG1420 5.0 31.9 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: Sun Jul 6 21:44:03 2025

Last articles

F in 4IKS
F in 4ISE
F in 4IQV
F in 4IQW
F in 4IQT
F in 4IQU
F in 4INB
F in 4IKT
F in 4IJU
F in 4IKL
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy