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Magnesium in PDB 1a95: Xprtase From E. Coli Complexed with Mg:Cprpp and Guanine

Enzymatic activity of Xprtase From E. Coli Complexed with Mg:Cprpp and Guanine

All present enzymatic activity of Xprtase From E. Coli Complexed with Mg:Cprpp and Guanine:
2.4.2.22;

Protein crystallography data

The structure of Xprtase From E. Coli Complexed with Mg:Cprpp and Guanine, PDB code: 1a95 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 / 2.00
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 94.200, 94.200, 165.900, 90.00, 90.00, 90.00
R / Rfree (%) 20.7 / 23.2

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Xprtase From E. Coli Complexed with Mg:Cprpp and Guanine (pdb code 1a95). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Xprtase From E. Coli Complexed with Mg:Cprpp and Guanine, PDB code: 1a95:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 1a95

Go back to Magnesium Binding Sites List in 1a95
Magnesium binding site 1 out of 2 in the Xprtase From E. Coli Complexed with Mg:Cprpp and Guanine


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Xprtase From E. Coli Complexed with Mg:Cprpp and Guanine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg308

b:43.9
occ:1.00
O B:HOH535 2.0 44.5 1.0
O3 B:PCP301 2.2 70.3 1.0
O B:HOH536 2.2 40.4 1.0
O1 B:PCP301 2.2 83.8 1.0
O2B B:PCP301 2.5 90.5 1.0
O2 B:PCP301 3.0 73.0 1.0
C3 B:PCP301 3.1 71.2 1.0
C1 B:PCP301 3.1 76.2 1.0
C2 B:PCP301 3.2 73.5 1.0
PA B:PCP301 3.2 89.1 1.0
O2A B:PCP301 3.3 89.4 1.0
PB B:PCP301 3.3 90.0 1.0
C5 B:PCP301 3.4 72.7 1.0
O3A B:PCP301 3.6 90.3 1.0
O1B B:PCP301 3.6 90.3 1.0
C4 B:PCP301 3.7 68.5 1.0
OD1 B:ASP88 4.1 16.9 1.0
N B:GLY38 4.1 15.5 1.0
O B:SER36 4.2 19.5 1.0
OD2 B:ASP88 4.3 16.3 1.0
N B:ARG37 4.4 17.4 1.0
O1A B:PCP301 4.5 89.1 1.0
CA B:GLY38 4.5 14.0 1.0
C B:SER36 4.6 17.8 1.0
CG B:ASP88 4.6 17.6 1.0
O3B B:PCP301 4.7 90.2 1.0
CG1 B:VAL35 4.7 9.8 1.0
OD1 B:ASP89 4.7 16.8 1.0
O B:VAL35 4.8 18.5 1.0

Magnesium binding site 2 out of 2 in 1a95

Go back to Magnesium Binding Sites List in 1a95
Magnesium binding site 2 out of 2 in the Xprtase From E. Coli Complexed with Mg:Cprpp and Guanine


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Xprtase From E. Coli Complexed with Mg:Cprpp and Guanine within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg307

b:36.9
occ:1.00
O C:HOH533 2.0 38.3 1.0
O3 C:PCP302 2.2 57.1 1.0
O C:HOH534 2.2 37.8 1.0
O1 C:PCP302 2.3 67.3 1.0
O2B C:PCP302 2.3 67.7 1.0
O2 C:PCP302 2.6 59.7 1.0
C2 C:PCP302 3.0 59.7 1.0
C3 C:PCP302 3.0 57.9 1.0
C1 C:PCP302 3.1 61.9 1.0
PB C:PCP302 3.4 66.9 1.0
PA C:PCP302 3.5 71.5 1.0
C5 C:PCP302 3.6 59.5 1.0
O3A C:PCP302 3.7 70.5 1.0
O2A C:PCP302 3.7 71.3 1.0
O1B C:PCP302 3.8 66.1 1.0
N C:GLY38 3.8 16.9 1.0
C4 C:PCP302 3.8 55.8 1.0
OD1 C:ASP88 3.9 13.6 1.0
OD1 C:ASP89 4.1 24.4 1.0
CA C:GLY38 4.1 17.4 1.0
N C:ARG37 4.2 17.8 1.0
O C:SER36 4.3 19.4 1.0
OD2 C:ASP88 4.5 15.4 1.0
C C:SER36 4.6 19.0 1.0
O3B C:PCP302 4.6 68.9 1.0
CG C:ASP88 4.6 14.8 1.0
O1A C:PCP302 4.7 72.1 1.0
O C:VAL35 4.7 22.1 1.0
O C:HOH421 4.8 37.3 1.0
C C:ARG37 4.9 18.1 1.0

Reference:

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
Page generated: Mon Dec 14 03:28:22 2020

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