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Magnesium in PDB 1vjc: Structure of Pig Muscle Pgk Complexed with Mgatp

Enzymatic activity of Structure of Pig Muscle Pgk Complexed with Mgatp

All present enzymatic activity of Structure of Pig Muscle Pgk Complexed with Mgatp:
2.7.2.3;

Protein crystallography data

The structure of Structure of Pig Muscle Pgk Complexed with Mgatp, PDB code: 1vjc was solved by B.Flachner, Z.Kovari, A.Varga, Z.Gugolya, F.Vonderviszt, G.Naray-Szabo, M.Vas, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 27.00 / 2.10
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 36.200, 106.500, 51.100, 90.00, 97.60, 90.00
R / Rfree (%) 17.3 / 23.3

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of Pig Muscle Pgk Complexed with Mgatp (pdb code 1vjc). 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 Structure of Pig Muscle Pgk Complexed with Mgatp, PDB code: 1vjc:

Magnesium binding site 1 out of 1 in 1vjc

Go back to Magnesium Binding Sites List in 1vjc
Magnesium binding site 1 out of 1 in the Structure of Pig Muscle Pgk Complexed with Mgatp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Pig Muscle Pgk Complexed with Mgatp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg418

b:63.9
occ:1.00
O1B A:ATP417 2.1 63.4 1.0
O1G A:ATP417 2.4 65.6 1.0
O3B A:ATP417 3.0 64.6 1.0
PB A:ATP417 3.1 64.8 1.0
PG A:ATP417 3.3 67.6 1.0
O A:HOH535 3.3 40.8 1.0
O2G A:ATP417 3.8 66.5 1.0
O2B A:ATP417 4.0 62.4 1.0
O3A A:ATP417 4.3 61.4 1.0
O3G A:ATP417 4.6 64.5 1.0

Reference:

B.Flachner, A.Varga, Z.Gugolya, F.Vonderviszt, M.Vas. Role of Phosphate Chain Mobility of Mgatp in Completing the 3-Phosphoglycerate Kinase Catalytic Site: Binding, Kinetic, and Crystallographic Studies with Atp and Mgatp. Biochemistry V. 43 3436 2004.
ISSN: ISSN 0006-2960
PubMed: 15035615
DOI: 10.1021/BI035022N
Page generated: Tue Aug 13 15:05:14 2024

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