Phosphorus in PDB 1a9o: Bovine Purine Nucleoside Phosphorylase Complexed with Phosphate

All present enzymatic activity of Bovine Purine Nucleoside Phosphorylase Complexed with Phosphate:
2.4.2.1;

The structure of Bovine Purine Nucleoside Phosphorylase Complexed with Phosphate, PDB code: 1a9o was solved by C.Mao, W.J.Cook, M.Zhou, A.A.Fedorov, S.C.Almo, S.E.Ealick, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.00
Space group	P 21 3
Cell size a, b, c (Å), α, β, γ (°)	94.200, 94.200, 94.200, 90.00, 90.00, 90.00
R / Rfree (%)	20 / n/a

The binding sites of Phosphorus atom in the Bovine Purine Nucleoside Phosphorylase Complexed with Phosphate (pdb code 1a9o). This binding sites where shown within 5.0 Angstroms radius around Phosphorus atom.
In total only one binding site of Phosphorus was determined in the Bovine Purine Nucleoside Phosphorylase Complexed with Phosphate, PDB code: 1a9o:

Phosphorus binding site 1 out of 1 in the Bovine Purine Nucleoside Phosphorylase Complexed with Phosphate


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 1 of Bovine Purine Nucleoside Phosphorylase Complexed with Phosphate within 5.0Å range: probe atom residue distance (Å) B Occ A:P291 b:11.4 occ:0.71 P A:PO4291 0.0 11.4 0.7 O2 A:PO4291 1.4 12.0 0.7 O1 A:PO4291 1.4 11.5 0.7 O4 A:PO4291 1.4 11.2 0.7 O3 A:PO4291 1.4 12.1 0.7 NH1 A:ARG84 3.5 2.0 1.0 OG A:SER220 3.6 11.7 1.0 NE2 A:HIS86 4.0 8.2 1.0 CB A:ASN115 4.0 2.4 1.0 N A:ALA116 4.2 2.0 1.0 CA A:ASN115 4.2 4.9 1.0 CA A:GLY32 4.2 35.9 1.0 OG A:SER33 4.2 52.8 1.0 CD A:ARG84 4.4 12.2 1.0 CZ A:ARG84 4.5 11.3 1.0 C A:GLY32 4.6 41.6 1.0 N A:SER33 4.6 46.3 1.0 CB A:SER220 4.7 8.2 1.0 C A:ASN115 4.7 5.6 1.0 O A:ALA116 4.8 6.3 1.0 NE A:ARG84 4.9 7.3 1.0 CE1 A:HIS86 4.9 12.0 1.0 CG A:ARG84 4.9 10.7 1.0 CD2 A:HIS86 4.9 8.6 1.0

C.Mao, W.J.Cook, M.Zhou, A.A.Federov, S.C.Almo, S.E.Ealick. Calf Spleen Purine Nucleoside Phosphorylase Complexed with Substrates and Substrate Analogues. Biochemistry V. 37 7135 1998.
ISSN: ISSN 0006-2960
PubMed: 9585525
DOI: 10.1021/BI9723919