Atomistry » Aluminium » PDB 1vfx-2x2f » 2wzc
Atomistry »
  Aluminium »
    PDB 1vfx-2x2f »
      2wzc »

Aluminium in PDB 2wzc: The Catalytically Active Fully Closed Conformation of Human Phosphoglycerate Kinase in Complex with Adp, 3PG and Aluminium Tetrafluoride

Enzymatic activity of The Catalytically Active Fully Closed Conformation of Human Phosphoglycerate Kinase in Complex with Adp, 3PG and Aluminium Tetrafluoride

All present enzymatic activity of The Catalytically Active Fully Closed Conformation of Human Phosphoglycerate Kinase in Complex with Adp, 3PG and Aluminium Tetrafluoride:
2.7.2.3;

Protein crystallography data

The structure of The Catalytically Active Fully Closed Conformation of Human Phosphoglycerate Kinase in Complex with Adp, 3PG and Aluminium Tetrafluoride, PDB code: 2wzc was solved by M.W.Bowler, M.J.Cliff, J.P.M.Marston, N.J.Baxter, A.M.H.Hownslow, A.V.Varga, J.Szabo, M.Vas, G.M.Blackburn, J.P.Waltho, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.50
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 39.220, 91.920, 108.140, 90.00, 90.00, 90.00
R / Rfree (%) 16.415 / 19.763

Other elements in 2wzc:

The structure of The Catalytically Active Fully Closed Conformation of Human Phosphoglycerate Kinase in Complex with Adp, 3PG and Aluminium Tetrafluoride also contains other interesting chemical elements:

Fluorine (F) 4 atoms
Magnesium (Mg) 1 atom
Chlorine (Cl) 1 atom

Aluminium Binding Sites:

The binding sites of Aluminium atom in the The Catalytically Active Fully Closed Conformation of Human Phosphoglycerate Kinase in Complex with Adp, 3PG and Aluminium Tetrafluoride (pdb code 2wzc). This binding sites where shown within 5.0 Angstroms radius around Aluminium atom.
In total only one binding site of Aluminium was determined in the The Catalytically Active Fully Closed Conformation of Human Phosphoglycerate Kinase in Complex with Adp, 3PG and Aluminium Tetrafluoride, PDB code: 2wzc:

Aluminium binding site 1 out of 1 in 2wzc

Go back to Aluminium Binding Sites List in 2wzc
Aluminium binding site 1 out of 1 in the The Catalytically Active Fully Closed Conformation of Human Phosphoglycerate Kinase in Complex with Adp, 3PG and 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 Catalytically Active Fully Closed Conformation of Human Phosphoglycerate Kinase in Complex with Adp, 3PG and Aluminium Tetrafluoride within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Al1419

b:9.2
occ:1.00
AL A:ALF1419 0.0 9.2 1.0
F2 A:ALF1419 1.8 10.3 1.0
F3 A:ALF1419 1.8 9.6 1.0
F4 A:ALF1419 1.8 10.9 1.0
F1 A:ALF1419 1.8 7.8 1.0
O2 A:3PG1421 1.9 9.5 1.0
O3B A:ADP1420 2.0 8.8 1.0
C1 A:3PG1421 2.9 7.7 1.0
PB A:ADP1420 3.2 8.3 1.0
O1 A:3PG1421 3.2 9.8 1.0
O1B A:ADP1420 3.4 8.8 1.0
MG A:MG1417 3.6 8.9 1.0
NZ A:LYS215 3.8 6.0 1.0
O A:HOH2470 3.8 3.5 1.0
NZ A:LYS219 3.9 6.6 1.0
O A:HOH2471 3.9 5.3 1.0
O A:HOH2213 4.1 4.3 1.0
O1A A:ADP1420 4.2 8.3 1.0
N A:GLY396 4.2 6.0 1.0
O3A A:ADP1420 4.2 8.5 1.0
NH2 A:ARG38 4.2 5.5 1.0
C2 A:3PG1421 4.2 8.9 1.0
O2B A:ADP1420 4.3 8.8 1.0
N A:GLY373 4.3 4.7 1.0
CA A:GLY372 4.5 5.3 1.0
PA A:ADP1420 4.5 9.0 1.0
CA A:GLY395 4.6 5.8 1.0
CE A:LYS215 4.7 6.6 1.0
CD A:LYS215 4.7 6.4 1.0
ND2 A:ASN336 4.7 5.8 1.0
CE A:LYS219 4.8 7.2 1.0
N A:GLY395 4.8 5.8 1.0
O A:HOH2464 4.8 7.5 1.0
O2A A:ADP1420 4.8 10.1 1.0
C3 A:3PG1421 4.9 8.4 1.0
C A:GLY395 4.9 5.4 1.0
C A:GLY372 4.9 5.6 1.0

Reference:

M.J.Cliff, M.W.Bowler, J.Szabo, J.P.M.Marston, A.V.Varga, A.M.H.Hownslow, N.J.Baxter, G.M.Blackburn, M.Vas, J.P.Waltho. Transition State Analogue Structures of Human Phosphoglycerate Kinase Establish the Importance of Charge Balance in Catalysis. J.Am.Chem.Soc. V. 132 6507 2010.
ISSN: ISSN 0002-7863
PubMed: 20397725
DOI: 10.1021/JA100974T
Page generated: Wed Jul 10 09:33:14 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy