Calcium in PDB 1zmr: Crystal Structure of the E. Coli Phosphoglycerate Kinase

All present enzymatic activity of Crystal Structure of the E. Coli Phosphoglycerate Kinase:
2.7.2.3;

The structure of Crystal Structure of the E. Coli Phosphoglycerate Kinase, PDB code: 1zmr was solved by S.Marqusee, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.40
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	77.887, 77.887, 195.276, 90.00, 90.00, 120.00
R / Rfree (%)	21.9 / 25.3

The binding sites of Calcium atom in the Crystal Structure of the E. Coli Phosphoglycerate Kinase (pdb code 1zmr). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 3 binding sites of Calcium where determined in the Crystal Structure of the E. Coli Phosphoglycerate Kinase, PDB code: 1zmr:
Jump to Calcium binding site number: 1; 2; 3;

Calcium binding site 1 out of 3 in the Crystal Structure of the E. Coli Phosphoglycerate Kinase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of the E. Coli Phosphoglycerate Kinase within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca401 b:41.8 occ:1.00 O A:ASP237 2.4 40.6 1.0 O A:HOH491 2.4 35.0 1.0 OD1 A:ASP240 2.8 38.6 1.0 OD2 A:ASP240 2.8 38.3 1.0 CG A:ASP240 3.1 38.7 1.0 C A:ASP237 3.4 40.7 1.0 O A:HOH471 4.1 39.7 1.0 CA A:ASP237 4.3 41.1 1.0 OE2 A:GLU241 4.3 39.5 1.0 N A:LEU238 4.4 40.4 1.0 CA A:LEU238 4.5 40.1 1.0 CB A:ASP237 4.6 41.1 1.0 CB A:ASP240 4.6 38.9 1.0 CG A:GLU241 4.7 39.3 1.0

Calcium binding site 2 out of 3 in the Crystal Structure of the E. Coli Phosphoglycerate Kinase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure of the E. Coli Phosphoglycerate Kinase within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca402 b:45.3 occ:1.00 O A:HOH510 2.4 46.0 1.0 O A:LYS84 2.4 41.9 1.0 O A:HOH546 2.4 45.7 1.0 O A:HOH564 2.6 57.3 1.0 C A:LYS84 3.5 42.0 1.0 N A:LEU85 4.3 42.1 1.0 CA A:LEU85 4.3 42.2 1.0 CA A:LYS84 4.4 41.9 1.0 CD1 A:LEU85 4.5 42.0 1.0 O A:HOH408 4.5 28.1 1.0 OE2 A:GLU45 4.5 39.5 1.0 O A:HOH579 4.7 51.8 1.0 OE1 A:GLU45 4.9 39.7 1.0 CB A:LYS84 5.0 41.9 1.0

Calcium binding site 3 out of 3 in the Crystal Structure of the E. Coli Phosphoglycerate Kinase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of Crystal Structure of the E. Coli Phosphoglycerate Kinase within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca403 b:50.2 occ:1.00 O A:LYS82 2.4 41.2 1.0 O A:HOH531 2.4 50.5 1.0 O A:LEU85 2.5 42.4 1.0 C A:LYS82 3.5 41.2 1.0 C A:LEU85 3.7 42.4 1.0 CA A:LYS82 4.0 41.2 1.0 CA A:SER86 4.4 43.0 1.0 O A:ASN87 4.4 43.7 1.0 O A:SER86 4.5 43.2 1.0 CB A:LYS82 4.5 41.2 1.0 N A:SER86 4.5 42.7 1.0 O A:HOH483 4.5 44.2 1.0 C A:SER86 4.5 43.1 1.0 N A:ASP83 4.6 41.4 1.0 CA A:LEU85 4.8 42.2 1.0 N A:LEU85 4.8 42.1 1.0 CA A:ASP83 4.9 41.5 1.0

T.A.Young, E.Skordalakes, S.Marqusee. Comparison of Proteolytic Susceptibility in Phosphoglycerate Kinases From Yeast and E. Coli: Modulation of Conformational Ensembles Without Altering Structure or Stability. J.Mol.Biol. V. 368 1438 2007.
ISSN: ISSN 0022-2836
PubMed: 17397866
DOI: 10.1016/J.JMB.2007.02.077