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Magnesium in PDB 1vpe: Crystallographic Analysis of Phosphoglycerate Kinase From the Hyperthermophilic Bacterium Thermotoga Maritima

Enzymatic activity of Crystallographic Analysis of Phosphoglycerate Kinase From the Hyperthermophilic Bacterium Thermotoga Maritima

All present enzymatic activity of Crystallographic Analysis of Phosphoglycerate Kinase From the Hyperthermophilic Bacterium Thermotoga Maritima:
2.7.2.3;

Protein crystallography data

The structure of Crystallographic Analysis of Phosphoglycerate Kinase From the Hyperthermophilic Bacterium Thermotoga Maritima, PDB code: 1vpe was solved by G.Auerbach, R.Huber, M.Graettinger, K.Zaiss, H.Schurig, R.Jaenicke, U.Jacob, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 2.00
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 62.009, 76.864, 87.501, 90.00, 90.00, 90.00
R / Rfree (%) 19.8 / 28.8

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystallographic Analysis of Phosphoglycerate Kinase From the Hyperthermophilic Bacterium Thermotoga Maritima (pdb code 1vpe). 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 Crystallographic Analysis of Phosphoglycerate Kinase From the Hyperthermophilic Bacterium Thermotoga Maritima, PDB code: 1vpe:

Magnesium binding site 1 out of 1 in 1vpe

Go back to Magnesium Binding Sites List in 1vpe
Magnesium binding site 1 out of 1 in the Crystallographic Analysis of Phosphoglycerate Kinase From the Hyperthermophilic Bacterium Thermotoga Maritima


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystallographic Analysis of Phosphoglycerate Kinase From the Hyperthermophilic Bacterium Thermotoga Maritima within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg402

b:33.3
occ:1.00
 O A:HOH626 1.8 36.5 1.0
O A:HOH627 1.9 34.3 1.0
O1B A:ANP400 2.0 26.1 1.0
O A:HOH628 2.1 44.4 1.0
O2A A:ANP400 2.2 36.8 1.0
O1G A:ANP400 2.4 37.0 1.0
PB A:ANP400 3.1 26.7 1.0
PG A:ANP400 3.1 37.8 1.0
N3B A:ANP400 3.3 27.4 1.0
PA A:ANP400 3.3 31.5 1.0
O2G A:ANP400 3.4 40.2 1.0
O3A A:ANP400 3.5 31.7 1.0
OD2 A:ASP355 3.9 35.8 1.0
O A:HOH459 4.1 47.9 1.0
O5' A:ANP400 4.3 36.7 1.0
O1A A:ANP400 4.3 38.5 1.0
N A:GLY354 4.3 18.5 1.0
N A:ASP355 4.4 27.6 1.0
O2B A:ANP400 4.4 20.3 1.0
O A:HOH406 4.5 74.3 1.0
O3G A:ANP400 4.5 39.3 1.0
CA A:GLY354 4.5 22.7 1.0
CG A:ASP355 4.7 36.7 1.0
CD A:LYS197 4.8 78.2 1.0

Reference:

G.Auerbach, R.Huber, M.Grattinger, K.Zaiss, H.Schurig, R.Jaenicke, U.Jacob. Closed Structure of Phosphoglycerate Kinase From Thermotoga Maritima Reveals the Catalytic Mechanism and Determinants of Thermal Stability. Structure V. 5 1475 1997.
ISSN: ISSN 0969-2126
PubMed: 9384563
DOI: 10.1016/S0969-2126(97)00297-9
Page generated: Sun Aug 10 05:17:55 2025

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