Atomistry » Magnesium » PDB 2x13-2xbn » 2x15
Atomistry »
  Magnesium »
    PDB 2x13-2xbn »
      2x15 »

Magnesium in PDB 2x15: The Catalytically Active Fully Closed Conformation of Human Phosphoglycerate Kinase in Complex with Adp and 1,3- Bisphosphoglycerate

Enzymatic activity of The Catalytically Active Fully Closed Conformation of Human Phosphoglycerate Kinase in Complex with Adp and 1,3- Bisphosphoglycerate

All present enzymatic activity of The Catalytically Active Fully Closed Conformation of Human Phosphoglycerate Kinase in Complex with Adp and 1,3- Bisphosphoglycerate:
2.7.2.3;

Protein crystallography data

The structure of The Catalytically Active Fully Closed Conformation of Human Phosphoglycerate Kinase in Complex with Adp and 1,3- Bisphosphoglycerate, PDB code: 2x15 was solved by M.W.Bowler, M.J.Cliff, J.P.M.Marston, N.J.Baxter, A.M.H.Hounslow, 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 / 2.10
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 38.730, 91.750, 108.310, 90.00, 90.00, 90.00
R / Rfree (%) 19.249 / 23.795

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 and 1,3- Bisphosphoglycerate (pdb code 2x15). 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 and 1,3- Bisphosphoglycerate, PDB code: 2x15:

Magnesium binding site 1 out of 1 in 2x15

Go back to Magnesium Binding Sites List in 2x15
Magnesium binding site 1 out of 1 in the The Catalytically Active Fully Closed Conformation of Human Phosphoglycerate Kinase in Complex with Adp and 1,3- Bisphosphoglycerate


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 and 1,3- Bisphosphoglycerate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1418

b:23.8
occ:1.00
 O1B A:ATP1422 1.8 12.6 0.2
O A:HOH2078 1.8 22.7 1.0
O2A A:ADP1419 2.0 14.9 0.8
O3B A:ADP1419 2.0 16.4 0.8
O1A A:ATP1422 2.0 8.5 0.2
O A:HOH2080 2.1 16.7 1.0
OD2 A:ASP375 2.4 15.3 1.0
OAH A:X151420 2.4 15.5 0.8
O3G A:ATP1422 2.6 10.3 0.2
PB A:ATP1422 2.9 12.2 0.2
PB A:ADP1419 3.1 18.5 0.8
PA A:ADP1419 3.3 15.0 0.8
PA A:ATP1422 3.3 8.0 0.2
O3A A:ATP1422 3.3 11.7 0.2
CG A:ASP375 3.4 13.9 1.0
O3B A:ATP1422 3.5 11.3 0.2
PG A:ATP1422 3.5 4.7 0.2
O3A A:ADP1419 3.5 15.9 0.8
O1B A:ADP1419 3.6 20.8 0.8
NZ A:LYS216 3.7 13.8 1.0
PAO A:X151420 3.9 16.1 0.8
CB A:ASP375 4.0 12.6 1.0
N A:ASP375 4.1 12.3 1.0
O A:HOH2066 4.1 18.7 1.0
O2B A:ATP1422 4.1 11.7 0.2
C5' A:ADP1419 4.1 17.8 0.8
C5' A:ATP1422 4.2 13.4 0.2
O5' A:ADP1419 4.2 15.9 0.8
OAB A:X151420 4.2 16.9 0.8
CE A:LYS216 4.2 14.7 1.0
O5' A:ATP1422 4.2 11.2 0.2
O1G A:ATP1422 4.2 8.8 0.2
OD1 A:ASP375 4.3 12.5 1.0
O2A A:ATP1422 4.3 9.4 0.2
O1 A:3PG1421 4.3 20.3 0.2
OAG A:X151420 4.3 12.9 0.8
O1A A:ADP1419 4.4 17.6 0.8
O2B A:ADP1419 4.4 16.9 0.8
O A:HOH2003 4.5 12.4 1.0
O A:HOH2065 4.6 11.1 1.0
CA A:ASP375 4.7 12.6 1.0
N A:GLY374 4.7 10.9 1.0
CD A:LYS216 4.8 11.7 1.0
OAF A:X151420 4.8 13.1 0.8
CA A:GLY374 4.8 11.3 1.0
O2G A:ATP1422 4.9 9.2 0.2
C A:GLY374 4.9 11.7 1.0
O A:HOH2036 4.9 6.9 1.0
O2 A:3PG1421 5.0 20.2 0.2

Reference:

M.W.Bowler, M.J.Cliff, J.P.M.Marston, N.J.Baxter, A.M.H.Hounslow, 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 Analoges To Be Published.
Page generated: Wed Aug 14 06:57:54 2024

Last articles

Ca in 2VDN
Ca in 2VDM
Ca in 2VDL
Ca in 2VDK
Ca in 2VC2
Ca in 2VCP
Ca in 2VBO
Ca in 2VCC
Ca in 2VCA
Ca in 2VCB
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy