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Magnesium 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
Aluminium (Al) 1 atom
Chlorine (Cl) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium 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 Magnesium atom.
In total only one binding site of Magnesium 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:

Magnesium binding site 1 out of 1 in 2wzc

Go back to Magnesium Binding Sites List in 2wzc
Magnesium 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 Magnesium with other atoms in the Mg 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:Mg1417

b:8.9
occ:1.00
 F1 A:ALF1419 2.0 7.8 1.0
O1B A:ADP1420 2.0 8.8 1.0
O1A A:ADP1420 2.1 8.3 1.0
OD2 A:ASP374 2.1 6.6 1.0
O A:HOH2464 2.1 7.5 1.0
O A:HOH2470 2.1 3.5 1.0
PB A:ADP1420 3.1 8.3 1.0
CG A:ASP374 3.2 7.6 1.0
PA A:ADP1420 3.3 9.0 1.0
O3A A:ADP1420 3.5 8.5 1.0
O3B A:ADP1420 3.6 8.8 1.0
AL A:ALF1419 3.6 9.2 1.0
F2 A:ALF1419 3.7 10.3 1.0
CB A:ASP374 3.8 6.4 1.0
O A:HOH2467 3.9 11.4 1.0
NZ A:LYS215 3.9 6.0 1.0
N A:ASP374 4.0 5.6 1.0
O1 A:3PG1421 4.1 9.8 1.0
O A:HOH2425 4.2 15.8 1.0
OD1 A:ASP374 4.2 6.8 1.0
C5' A:ADP1420 4.2 9.4 1.0
CE A:LYS215 4.2 6.6 1.0
O5' A:ADP1420 4.3 9.6 1.0
O A:HOH2197 4.3 13.4 1.0
F3 A:ALF1419 4.4 9.6 1.0
O A:HOH2040 4.4 6.6 1.0
O2B A:ADP1420 4.4 8.8 1.0
O2A A:ADP1420 4.4 10.1 1.0
O A:HOH2426 4.6 6.9 1.0
O2 A:3PG1421 4.6 9.5 1.0
CA A:ASP374 4.6 6.4 1.0
C1 A:3PG1421 4.8 7.7 1.0
N A:GLY373 4.8 4.7 1.0
CD A:LYS215 4.9 6.4 1.0
C A:GLY373 4.9 5.4 1.0
CA A:GLY373 4.9 5.7 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 Aug 14 06:19:39 2024

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