Calcium in PDB 1n7v: The Receptor-Binding Protein P2 of Bacteriophage PRD1: Crystal Form III

The structure of The Receptor-Binding Protein P2 of Bacteriophage PRD1: Crystal Form III, PDB code: 1n7v was solved by L.Xu, S.D.Benson, S.J.Butcher, D.H.Bamford, R.M.Burnett, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.11 / 2.20
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	46.500, 270.200, 137.200, 90.00, 90.00, 90.00
R / Rfree (%)	22.9 / 26.2

The binding sites of Calcium atom in the The Receptor-Binding Protein P2 of Bacteriophage PRD1: Crystal Form III (pdb code 1n7v). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the The Receptor-Binding Protein P2 of Bacteriophage PRD1: Crystal Form III, PDB code: 1n7v:

Calcium binding site 1 out of 1 in the The Receptor-Binding Protein P2 of Bacteriophage PRD1: Crystal Form III


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of The Receptor-Binding Protein P2 of Bacteriophage PRD1: Crystal Form III within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca601 b:55.1 occ:1.00 O A:HOH735 2.4 32.7 1.0 O A:SER462 2.4 29.1 1.0 O A:HOH734 2.4 39.0 1.0 O A:HOH832 2.4 41.5 1.0 OD1 A:ASP425 2.5 42.8 1.0 O A:LYS426 2.7 32.8 1.0 C A:SER462 3.5 32.5 1.0 C A:LYS426 3.6 29.9 1.0 CG A:ASP425 3.7 39.8 1.0 N A:LYS426 3.7 29.6 1.0 O A:HOH733 3.8 40.4 1.0 CA A:SER462 4.0 33.4 1.0 CA A:LYS426 4.2 29.6 1.0 OD2 A:ASP425 4.3 39.8 1.0 CB A:SER462 4.4 30.3 1.0 O A:SER464 4.6 33.7 1.0 N A:PHE463 4.6 32.3 1.0 N A:THR427 4.6 27.7 1.0 CB A:LYS426 4.6 30.4 1.0 C A:ASP425 4.7 31.7 1.0 CB A:ASP425 4.9 34.9 1.0 CA A:ASP425 4.9 32.8 1.0 CA A:PHE463 4.9 31.5 1.0 CA A:THR427 4.9 28.3 1.0

L.Xu, S.D.Benson, S.J.Butcher, D.H.Bamford, R.M.Burnett. The Receptor Binding Protein P2 of PRD1, A Virus Targeting Antibiotic-Resistant Bacteria, Has A Novel Fold Suggesting Multiple Functions. Structure V. 11 309 2003.
ISSN: ISSN 0969-2126
PubMed: 12623018
DOI: 10.1016/S0969-2126(03)00023-6