Magnesium in PDB 1hdi: Pig Muscle 3-Phosphoglycerate Kinase Complexed with 3-Pg and Mgadp.

All present enzymatic activity of Pig Muscle 3-Phosphoglycerate Kinase Complexed with 3-Pg and Mgadp.:
2.7.2.3;

The structure of Pig Muscle 3-Phosphoglycerate Kinase Complexed with 3-Pg and Mgadp., PDB code: 1hdi was solved by A.N.Szilagyi, M.Ghosh, E.Garman, M.Vas, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.80
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	50.500, 105.200, 35.900, 90.00, 98.40, 90.00
R / Rfree (%)	20.7 / 26.2

The binding sites of Magnesium atom in the Pig Muscle 3-Phosphoglycerate Kinase Complexed with 3-Pg and Mgadp. (pdb code 1hdi). 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 Pig Muscle 3-Phosphoglycerate Kinase Complexed with 3-Pg and Mgadp., PDB code: 1hdi:

Magnesium binding site 1 out of 1 in the Pig Muscle 3-Phosphoglycerate Kinase Complexed with 3-Pg and Mgadp.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Pig Muscle 3-Phosphoglycerate Kinase Complexed with 3-Pg and Mgadp. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg418 b:46.0 occ:1.00 OD1 A:ASP374 2.7 23.8 1.0 O1P A:AMP417 3.0 33.3 1.0 C5' A:AMP417 3.3 31.9 1.0 CG A:ASP374 3.4 23.4 1.0 O3P A:AMP417 3.5 37.8 1.0 OD2 A:ASP374 3.7 22.5 1.0 P A:AMP417 3.7 35.1 1.0 O5' A:AMP417 4.0 33.9 1.0 O A:HOH2182 4.2 26.9 1.0 O A:HOH2201 4.3 39.9 1.0 O A:HOH2204 4.3 32.5 1.0 C4' A:AMP417 4.5 29.1 1.0 CB A:ASP374 4.5 22.0 1.0 O A:HOH2064 4.6 36.3 1.0 C3' A:AMP417 4.9 27.9 1.0

A.N.Szilagyi, M.Ghosh, E.Garman, M.Vas. A 1.8 A Resolution Structure of Pig Muscle 3-Phosphoglycerate Kinase with Bound Mgadp and 3-Phosphoglycerate in Open Conformation: New Insight Into the Role of the Nucleotide in Domain Closure. J. Mol. Biol. V. 306 499 2001.
ISSN: ISSN 0022-2836
PubMed: 11178909
DOI: 10.1006/JMBI.2000.4294