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Magnesium in PDB 1gxb: Anthranilate Phosphoribosyltransferase in Complex with Pyrophosphate and Magnesium

Enzymatic activity of Anthranilate Phosphoribosyltransferase in Complex with Pyrophosphate and Magnesium

All present enzymatic activity of Anthranilate Phosphoribosyltransferase in Complex with Pyrophosphate and Magnesium:
2.4.2.18;

Protein crystallography data

The structure of Anthranilate Phosphoribosyltransferase in Complex with Pyrophosphate and Magnesium, PDB code: 1gxb was solved by O.Mayans, A.Ivens, L.J.Nissen, K.Kirschner, M.Wilmanns, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.65
Space group P 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 90.845, 65.467, 115.372, 90.00, 107.25, 90.00
R / Rfree (%) 22.3 / 29.7

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Anthranilate Phosphoribosyltransferase in Complex with Pyrophosphate and Magnesium (pdb code 1gxb). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Anthranilate Phosphoribosyltransferase in Complex with Pyrophosphate and Magnesium, PDB code: 1gxb:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in 1gxb

Go back to Magnesium Binding Sites List in 1gxb
Magnesium binding site 1 out of 3 in the Anthranilate Phosphoribosyltransferase in Complex with Pyrophosphate and Magnesium


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Anthranilate Phosphoribosyltransferase in Complex with Pyrophosphate and Magnesium within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1344

b:42.6
occ:1.00
O A:POP1346 1.9 21.2 1.0
OG A:SER91 2.0 52.9 1.0
OE2 A:GLU224 2.4 89.8 1.0
O A:HOH2035 2.5 75.9 1.0
P2 A:POP1346 2.6 21.2 1.0
O5 A:POP1346 2.6 21.2 1.0
O4 A:POP1346 2.8 21.2 1.0
CB A:SER91 3.1 48.4 1.0
P1 A:POP1346 3.3 21.2 1.0
O A:HOH2061 3.4 75.9 1.0
O A:ALA78 3.4 0.4 1.0
O1 A:POP1346 3.4 21.2 1.0
CD A:GLU224 3.6 87.8 1.0
OD2 A:ASP223 3.6 39.6 1.0
CA A:GLY79 3.7 63.7 1.0
O6 A:POP1346 4.0 21.2 1.0
C A:ALA78 4.1 0.3 1.0
O2 A:POP1346 4.2 21.2 1.0
N A:GLY79 4.3 61.0 1.0
O A:HOH2034 4.3 51.0 1.0
O3 A:POP1346 4.4 21.2 1.0
CA A:SER91 4.4 43.5 1.0
OE1 A:GLU224 4.4 89.3 1.0
CG A:ASP223 4.4 38.9 1.0
O A:ASP223 4.4 37.8 1.0
CG A:GLU224 4.5 85.6 1.0
N A:SER91 4.5 43.4 1.0
O A:THR77 4.6 53.2 1.0
OD1 A:ASP223 4.8 38.9 1.0

Magnesium binding site 2 out of 3 in 1gxb

Go back to Magnesium Binding Sites List in 1gxb
Magnesium binding site 2 out of 3 in the Anthranilate Phosphoribosyltransferase in Complex with Pyrophosphate and Magnesium


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Anthranilate Phosphoribosyltransferase in Complex with Pyrophosphate and Magnesium within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg1346

b:47.2
occ:1.00
OE2 C:GLU224 1.8 65.7 1.0
O2 C:POP1348 1.8 21.2 1.0
O5 C:POP1348 2.3 21.2 1.0
OG C:SER91 2.4 59.7 1.0
O C:HOH2018 2.9 75.9 1.0
O C:HOH2048 2.9 44.3 1.0
CD C:GLU224 2.9 65.8 1.0
P1 C:POP1348 2.9 21.2 1.0
OD2 C:ASP223 3.2 50.1 1.0
O C:POP1348 3.4 21.2 1.0
P2 C:POP1348 3.4 21.2 1.0
O3 C:POP1348 3.5 21.2 1.0
O C:ALA78 3.5 0.2 1.0
CB C:SER91 3.5 51.1 1.0
OE1 C:GLU224 3.6 67.9 1.0
O C:HOH2066 3.8 75.9 1.0
CG C:ASP223 3.9 47.9 1.0
OD1 C:ASP223 4.0 49.0 1.0
CG C:GLU224 4.1 66.0 1.0
CA C:GLY79 4.1 56.2 1.0
O C:ASP223 4.2 47.1 1.0
C C:ALA78 4.3 98.2 1.0
O1 C:POP1348 4.3 21.2 1.0
O4 C:POP1348 4.3 21.2 1.0
O6 C:POP1348 4.5 21.2 1.0
N C:GLY79 4.5 54.5 1.0
N C:SER91 4.5 46.0 1.0
CA C:SER91 4.6 46.6 1.0

Magnesium binding site 3 out of 3 in 1gxb

Go back to Magnesium Binding Sites List in 1gxb
Magnesium binding site 3 out of 3 in the Anthranilate Phosphoribosyltransferase in Complex with Pyrophosphate and Magnesium


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Anthranilate Phosphoribosyltransferase in Complex with Pyrophosphate and Magnesium within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg1350

b:59.8
occ:1.00
O2 D:POP1349 1.8 21.2 1.0
OE2 D:GLU224 1.8 86.6 1.0
OG D:SER91 2.4 68.7 1.0
CD D:GLU224 3.0 84.7 1.0
CA D:GLY79 3.0 77.7 1.0
O D:ASP223 3.1 89.3 1.0
P1 D:POP1349 3.2 21.2 1.0
OD2 D:ASP223 3.3 59.9 1.0
N D:GLY79 3.4 77.8 1.0
CG D:GLU224 3.6 84.0 1.0
O1 D:POP1349 3.7 21.2 1.0
CB D:SER91 3.7 66.4 1.0
C D:ALA78 3.8 0.4 1.0
CG D:ASP223 3.8 61.7 1.0
O D:ALA78 3.9 0.7 1.0
O6 D:POP1349 3.9 21.2 1.0
O D:HOH2035 3.9 39.5 1.0
OE1 D:GLU224 4.0 85.2 1.0
O D:POP1349 4.2 21.2 1.0
C D:ASP223 4.2 89.7 1.0
OD1 D:ASP223 4.2 63.5 1.0
O3 D:POP1349 4.3 21.2 1.0
C D:GLY79 4.4 77.8 1.0
O D:HOH2015 4.6 75.9 1.0
CB D:ASP223 4.6 62.8 1.0
CA D:ALA78 4.8 0.6 1.0
CA D:SER91 4.8 66.5 1.0
P2 D:POP1349 4.8 21.2 1.0
CB D:GLU224 4.8 83.1 1.0
O D:HOH2043 4.9 75.9 1.0
O D:THR77 4.9 63.9 1.0

Reference:

O.Mayans, A.Ivens, L.J.Nissen, K.Kirschner, M.Wilmanns. Structural Analysis of Two Enzymes Catalysing Reverse Metabolic Reactions Implies Common Ancestry Embo J. V. 21 3245 2002.
ISSN: ISSN 0261-4189
PubMed: 12093726
DOI: 10.1093/EMBOJ/CDF298
Page generated: Tue Aug 13 03:51:36 2024

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