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Magnesium in PDB 1kf0: Crystal Structure of Pig Muscle Phosphoglycerate Kinase Ternary Complex with Amp-Pcp and 3PG

Enzymatic activity of Crystal Structure of Pig Muscle Phosphoglycerate Kinase Ternary Complex with Amp-Pcp and 3PG

All present enzymatic activity of Crystal Structure of Pig Muscle Phosphoglycerate Kinase Ternary Complex with Amp-Pcp and 3PG:
2.7.2.3;

Protein crystallography data

The structure of Crystal Structure of Pig Muscle Phosphoglycerate Kinase Ternary Complex with Amp-Pcp and 3PG, PDB code: 1kf0 was solved by Z.Kovari, B.Flachner, G.Naray-Szabo, M.Vas, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.50
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 36.600, 110.300, 48.000, 90.00, 93.90, 90.00
R / Rfree (%) 17.3 / 25.2

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Pig Muscle Phosphoglycerate Kinase Ternary Complex with Amp-Pcp and 3PG (pdb code 1kf0). 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 Crystal Structure of Pig Muscle Phosphoglycerate Kinase Ternary Complex with Amp-Pcp and 3PG, PDB code: 1kf0:

Magnesium binding site 1 out of 1 in 1kf0

Go back to Magnesium Binding Sites List in 1kf0
Magnesium binding site 1 out of 1 in the Crystal Structure of Pig Muscle Phosphoglycerate Kinase Ternary 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 Crystal Structure of Pig Muscle Phosphoglycerate Kinase Ternary Complex with Amp-Pcp and 3PG within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg518

b:63.1
occ:1.00
O2B A:ACP418 2.2 63.1 1.0
OD1 A:ASP218 2.3 34.8 1.0
CG A:ASP218 3.4 34.8 1.0
PB A:ACP418 3.5 63.1 1.0
O1A A:ACP418 3.5 63.1 1.0
C3B A:ACP418 3.8 63.1 1.0
NZ A:LYS219 4.0 33.1 1.0
O3A A:ACP418 4.0 63.1 1.0
OD2 A:ASP218 4.1 34.8 1.0
PA A:ACP418 4.2 63.1 1.0
O3G A:ACP418 4.3 63.1 1.0
CB A:ASP218 4.6 10.9 1.0
O2A A:ACP418 4.6 63.1 1.0
O1B A:ACP418 4.8 63.1 1.0
PG A:ACP418 4.9 63.1 1.0

Reference:

Z.Kovari, B.Flachner, G.Naray-Szabo, M.Vas. Crystallographic and Thiol-Reactivity Studies on the Complex of Pig Muscle Phosphoglycerate Kinase with Atp Analogues: Correlation Between Nucleotide Binding Mode and Helix Flexibility. Biochemistry V. 41 8796 2002.
ISSN: ISSN 0006-2960
PubMed: 12102622
DOI: 10.1021/BI020210J
Page generated: Tue Aug 13 07:41:48 2024

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