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Magnesium in PDB 2x14: The Catalytically Active Fully Closed Conformation of Human Phosphoglycerate Kinase K219A Mutant in Complex with Amp-Pcp and 3PG

Enzymatic activity of The Catalytically Active Fully Closed Conformation of Human Phosphoglycerate Kinase K219A Mutant in Complex with Amp-Pcp and 3PG

All present enzymatic activity of The Catalytically Active Fully Closed Conformation of Human Phosphoglycerate Kinase K219A Mutant in Complex with Amp-Pcp and 3PG:
2.7.2.3;

Protein crystallography data

The structure of The Catalytically Active Fully Closed Conformation of Human Phosphoglycerate Kinase K219A Mutant in Complex with Amp-Pcp and 3PG, PDB code: 2x14 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 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 39.340, 91.630, 108.480, 90.00, 90.00, 90.00
R / Rfree (%) 18.708 / 22.81

Magnesium Binding Sites:

The binding sites of Magnesium atom in the The Catalytically Active Fully Closed Conformation of Human Phosphoglycerate Kinase K219A Mutant in Complex with Amp-Pcp and 3PG (pdb code 2x14). 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 K219A Mutant in Complex with Amp-Pcp and 3PG, PDB code: 2x14:

Magnesium binding site 1 out of 1 in 2x14

Go back to Magnesium Binding Sites List in 2x14
Magnesium binding site 1 out of 1 in the The Catalytically Active Fully Closed Conformation of Human Phosphoglycerate Kinase K219A Mutant in Complex with Amp-Pcp and 3PG


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 K219A Mutant in Complex with Amp-Pcp and 3PG within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1418

b:14.7
occ:1.00
 O2B A:ACP1420 1.9 11.1 1.0
O1A A:ACP1420 2.0 13.5 1.0
O A:HOH2217 2.0 9.5 1.0
OD2 A:ASP375 2.1 13.5 1.0
O A:HOH2208 2.1 10.9 1.0
O1G A:ACP1420 2.2 16.1 1.0
PB A:ACP1420 3.1 15.2 1.0
CG A:ASP375 3.2 19.3 1.0
PA A:ACP1420 3.3 14.1 1.0
PG A:ACP1420 3.3 17.2 1.0
O3A A:ACP1420 3.5 12.8 1.0
C3B A:ACP1420 3.8 14.1 1.0
O2G A:ACP1420 3.8 15.1 1.0
CB A:ASP375 3.8 17.5 1.0
O A:HOH2210 3.8 12.7 1.0
NZ A:LYS216 3.9 13.8 1.0
N A:ASP375 4.0 17.1 1.0
O1 A:3PG1419 4.2 14.3 1.0
O A:HOH2010 4.2 7.9 1.0
OD1 A:ASP375 4.3 15.1 1.0
CE A:LYS216 4.3 16.5 1.0
O2A A:ACP1420 4.3 16.0 1.0
O5' A:ACP1420 4.3 15.6 1.0
C5' A:ACP1420 4.4 13.0 1.0
O1B A:ACP1420 4.4 14.0 1.0
N A:GLY374 4.4 17.3 1.0
CA A:ASP375 4.6 17.6 1.0
O3G A:ACP1420 4.6 16.9 1.0
CD A:LYS216 4.8 16.4 1.0
CA A:GLY374 4.8 17.5 1.0
C A:GLY374 4.8 18.1 1.0
O A:HOH2214 4.9 22.1 1.0
O A:HOH2188 5.0 11.4 1.0

Reference:

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. The Structure of Human Phosphoglycerate Kinase in Its Fully Active Conformation in Complex with Ground State Analogues To Be Published.
Page generated: Wed Aug 14 06:57:54 2024

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