Phosphorus in PDB 1a97: Xprtase From E. Coli Complexed with Gmp

All present enzymatic activity of Xprtase From E. Coli Complexed with Gmp:
2.4.2.22;

The structure of Xprtase From E. Coli Complexed with Gmp, PDB code: 1a97 was solved by S.Vos, R.J.Parry, M.R.Burns, J.De Jersey, J.L.Martin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.60
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	94.042, 94.042, 166.914, 90.00, 90.00, 90.00
R / Rfree (%)	23.3 / 26.3

The binding sites of Phosphorus atom in the Xprtase From E. Coli Complexed with Gmp (pdb code 1a97). This binding sites where shown within 5.0 Angstroms radius around Phosphorus atom.
In total 2 binding sites of Phosphorus where determined in the Xprtase From E. Coli Complexed with Gmp, PDB code: 1a97:
Jump to Phosphorus binding site number: 1; 2;

Phosphorus binding site 1 out of 2 in the Xprtase From E. Coli Complexed with Gmp


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 1 of Xprtase From E. Coli Complexed with Gmp within 5.0Å range: probe atom residue distance (Å) B Occ B:P305 b:43.6 occ:1.00 P B:5GP305 0.0 43.6 1.0 O2P B:5GP305 1.5 47.4 1.0 O3P B:5GP305 1.5 45.9 1.0 O1P B:5GP305 1.5 43.9 1.0 O5' B:5GP305 1.6 45.9 1.0 C5' B:5GP305 2.6 49.5 1.0 N B:THR93 3.4 33.0 1.0 OG1 B:THR93 3.5 31.0 1.0 CB B:ASP92 3.6 37.9 1.0 NH2 B:ARG69 3.7 56.7 0.5 C4' B:5GP305 3.8 52.1 1.0 OG1 B:THR96 3.8 21.8 1.0 NH1 B:ARG69 3.8 55.5 0.5 N B:ASP92 3.9 32.1 1.0 N B:GLY94 4.0 29.2 1.0 CA B:ASP92 4.1 33.8 1.0 CZ B:ARG69 4.2 55.4 0.5 C B:ASP92 4.3 33.8 1.0 CA B:THR93 4.3 31.3 1.0 N B:THR96 4.3 26.9 1.0 CB B:THR93 4.3 31.5 1.0 CB B:THR96 4.4 21.9 1.0 N B:GLY95 4.4 27.5 1.0 O4' B:5GP305 4.5 52.8 1.0 C B:THR93 4.6 31.1 1.0 CG B:ASP92 4.6 42.7 1.0 CG2 B:THR93 4.6 29.4 1.0 OD2 B:ASP92 4.8 47.2 1.0 CA B:GLY94 4.9 27.5 1.0 C3' B:5GP305 4.9 53.4 1.0

Phosphorus binding site 2 out of 2 in the Xprtase From E. Coli Complexed with Gmp


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 2 of Xprtase From E. Coli Complexed with Gmp within 5.0Å range: probe atom residue distance (Å) B Occ C:P306 b:53.1 occ:1.00 P C:5GP306 0.0 53.1 1.0 O2P C:5GP306 1.5 51.4 1.0 O3P C:5GP306 1.5 52.7 1.0 O1P C:5GP306 1.5 51.3 1.0 O5' C:5GP306 1.6 53.1 1.0 C5' C:5GP306 2.6 56.8 1.0 NH2 C:ARG69 3.4 55.8 1.0 OG1 C:THR93 3.6 28.9 1.0 N C:THR93 3.7 28.1 1.0 C4' C:5GP306 3.8 58.7 1.0 N C:GLY94 3.9 26.2 1.0 OG1 C:THR96 3.9 34.4 1.0 NH1 C:ARG69 3.9 55.2 1.0 N C:GLY95 3.9 26.8 1.0 CB C:ASP92 4.0 30.1 1.0 CZ C:ARG69 4.1 55.4 1.0 N C:ASP92 4.1 28.1 1.0 N C:THR96 4.1 30.0 1.0 CA C:ASP92 4.4 27.9 1.0 O4' C:5GP306 4.5 60.6 1.0 CA C:THR93 4.5 28.3 1.0 CB C:THR96 4.6 31.1 1.0 C C:ASP92 4.6 28.1 1.0 CA C:GLY95 4.6 28.0 1.0 CB C:THR93 4.6 29.1 1.0 CA C:GLY94 4.6 26.5 1.0 C C:GLY94 4.7 27.5 1.0 C C:THR93 4.7 27.9 1.0 C3' C:5GP306 4.9 59.4 1.0 C C:GLY95 4.9 28.9 1.0

S.Vos, R.J.Parry, M.R.Burns, J.De Jersey, J.L.Martin. Structures of Free and Complexed Forms of Escherichia Coli Xanthine-Guanine Phosphoribosyltransferase. J.Mol.Biol. V. 282 875 1998.
ISSN: ISSN 0022-2836
PubMed: 9743633
DOI: 10.1006/JMBI.1998.2051