Atomistry » Magnesium » PDB 4mpo-4naa » 4n5v
Atomistry »
  Magnesium »
    PDB 4mpo-4naa »
      4n5v »

Magnesium in PDB 4n5v: Alternative Substrates of Mycobacterium Tuberculosis Anthranilate Phosphoribosyl Transferase

Enzymatic activity of Alternative Substrates of Mycobacterium Tuberculosis Anthranilate Phosphoribosyl Transferase

All present enzymatic activity of Alternative Substrates of Mycobacterium Tuberculosis Anthranilate Phosphoribosyl Transferase:
2.4.2.18;

Protein crystallography data

The structure of Alternative Substrates of Mycobacterium Tuberculosis Anthranilate Phosphoribosyl Transferase, PDB code: 4n5v was solved by A.Castell, T.V.M.Cookson, E.J.Parker, E.N.Baker, S.J.Lott, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 73.52 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 79.595, 92.542, 121.063, 90.00, 90.00, 90.00
R / Rfree (%) 18.2 / 21.8

Other elements in 4n5v:

The structure of Alternative Substrates of Mycobacterium Tuberculosis Anthranilate Phosphoribosyl Transferase also contains other interesting chemical elements:

Fluorine (F) 4 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Alternative Substrates of Mycobacterium Tuberculosis Anthranilate Phosphoribosyl Transferase (pdb code 4n5v). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Alternative Substrates of Mycobacterium Tuberculosis Anthranilate Phosphoribosyl Transferase, PDB code: 4n5v:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 4n5v

Go back to Magnesium Binding Sites List in 4n5v
Magnesium binding site 1 out of 4 in the Alternative Substrates of Mycobacterium Tuberculosis Anthranilate Phosphoribosyl Transferase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Alternative Substrates of Mycobacterium Tuberculosis Anthranilate Phosphoribosyl Transferase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg402

b:20.2
occ:1.00
 O2B A:PRP401 2.1 19.9 1.0
O2A A:PRP401 2.1 16.5 1.0
O A:HOH507 2.1 18.9 1.0
OE2 A:GLU252 2.1 21.2 1.0
OG A:SER119 2.2 19.2 1.0
O A:HOH504 2.2 18.0 1.0
CD A:GLU252 3.1 25.0 1.0
CB A:SER119 3.1 17.7 1.0
PA A:PRP401 3.3 22.8 1.0
PB A:PRP401 3.3 20.9 1.0
OE1 A:GLU252 3.3 24.5 1.0
MG A:MG403 3.4 37.4 1.0
O3A A:PRP401 3.5 23.7 1.0
N A:GLY107 3.8 18.0 1.0
OD2 A:ASP251 3.9 23.1 1.0
O A:HOH572 4.0 28.9 1.0
N A:SER119 4.0 19.4 1.0
CA A:SER119 4.1 18.8 1.0
O4 A:PRP401 4.2 27.1 1.0
O A:ASP251 4.2 21.6 1.0
O1A A:PRP401 4.3 26.4 1.0
CA A:GLY107 4.3 17.0 1.0
O1B A:PRP401 4.3 20.3 1.0
O3B A:PRP401 4.3 23.9 1.0
O1 A:PRP401 4.4 25.9 1.0
O A:HOH534 4.4 27.6 1.0
OD1 A:ASP251 4.4 24.3 1.0
CG A:ASP251 4.4 24.0 1.0
CG A:GLU252 4.4 21.7 1.0
O A:HOH734 4.5 48.2 1.0
C1 A:PRP401 4.5 22.4 1.0
C A:VAL106 4.6 17.1 1.0
CA A:VAL106 4.8 17.6 1.0

Magnesium binding site 2 out of 4 in 4n5v

Go back to Magnesium Binding Sites List in 4n5v
Magnesium binding site 2 out of 4 in the Alternative Substrates of Mycobacterium Tuberculosis Anthranilate Phosphoribosyl Transferase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Alternative Substrates of Mycobacterium Tuberculosis Anthranilate Phosphoribosyl Transferase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg403

b:37.4
occ:1.00
 O A:HOH507 2.3 18.9 1.0
OD1 A:ASP251 2.3 24.3 1.0
O A:HOH734 2.4 48.2 1.0
OE2 A:GLU252 2.4 21.2 1.0
O A:HOH572 2.4 28.9 1.0
O A:HOH740 2.4 42.1 1.0
CG A:ASP251 3.3 24.0 1.0
CD A:GLU252 3.4 25.0 1.0
MG A:MG402 3.4 20.2 1.0
OD2 A:ASP251 3.5 23.1 1.0
O A:HOH773 3.5 49.1 1.0
O2B A:PRP401 3.6 19.9 1.0
CG A:GLU252 3.6 21.7 1.0
OD2 A:ASP111 3.9 29.6 1.0
O A:HOH504 4.3 18.0 1.0
O A:HOH680 4.3 43.9 1.0
OG1 A:THR115 4.4 31.6 1.0
O A:ASP251 4.4 21.6 1.0
O3B A:PRP401 4.5 23.9 1.0
OE1 A:GLU252 4.5 24.5 1.0
CG A:ASP111 4.6 29.1 1.0
CB A:ASP251 4.7 21.8 1.0
PB A:PRP401 4.7 20.9 1.0
O4 A:PRP401 4.7 27.1 1.0
C A:ASP251 4.7 22.0 1.0
N A:ASP251 4.8 21.9 1.0
OD1 A:ASP111 4.9 28.3 1.0
O2A A:PRP401 4.9 16.5 1.0
CA A:ASP251 5.0 22.2 1.0

Magnesium binding site 3 out of 4 in 4n5v

Go back to Magnesium Binding Sites List in 4n5v
Magnesium binding site 3 out of 4 in the Alternative Substrates of Mycobacterium Tuberculosis Anthranilate Phosphoribosyl Transferase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Alternative Substrates of Mycobacterium Tuberculosis Anthranilate Phosphoribosyl Transferase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg402

b:23.2
occ:1.00
 O3B B:PRP401 2.0 21.7 1.0
O B:HOH503 2.1 18.4 1.0
O1A B:PRP401 2.1 22.6 1.0
OG B:SER119 2.1 21.6 1.0
OE2 B:GLU252 2.2 25.9 1.0
O B:HOH508 2.2 19.6 1.0
CB B:SER119 3.0 19.9 1.0
CD B:GLU252 3.1 26.0 1.0
PB B:PRP401 3.2 23.6 1.0
PA B:PRP401 3.2 24.5 1.0
OE1 B:GLU252 3.4 27.0 1.0
MG B:MG403 3.5 36.5 1.0
O3A B:PRP401 3.5 27.0 1.0
O B:HOH536 3.8 26.7 1.0
OD2 B:ASP251 3.9 27.8 1.0
N B:GLY107 3.9 20.0 1.0
N B:SER119 4.0 20.3 1.0
CA B:SER119 4.1 20.3 1.0
O4 B:PRP401 4.2 34.0 1.0
O B:ASP251 4.2 25.9 1.0
O B:HOH547 4.2 25.7 1.0
O2A B:PRP401 4.3 31.4 1.0
O1B B:PRP401 4.3 25.7 1.0
O1 B:PRP401 4.4 31.2 1.0
O2B B:PRP401 4.4 22.1 1.0
CG B:ASP251 4.4 27.6 1.0
CA B:GLY107 4.4 20.6 1.0
OD1 B:ASP251 4.4 28.3 1.0
CG B:GLU252 4.5 26.7 1.0
C1 B:PRP401 4.6 30.3 1.0
C B:VAL106 4.6 20.7 1.0
CA B:VAL106 4.9 20.5 1.0

Magnesium binding site 4 out of 4 in 4n5v

Go back to Magnesium Binding Sites List in 4n5v
Magnesium binding site 4 out of 4 in the Alternative Substrates of Mycobacterium Tuberculosis Anthranilate Phosphoribosyl Transferase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Alternative Substrates of Mycobacterium Tuberculosis Anthranilate Phosphoribosyl Transferase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg403

b:36.5
occ:1.00
 OD1 B:ASP251 2.3 28.3 1.0
OE2 B:GLU252 2.4 25.9 1.0
O B:HOH681 2.4 38.7 1.0
O B:HOH536 2.5 26.7 1.0
O B:HOH508 2.5 19.6 1.0
CG B:ASP251 3.3 27.6 1.0
CD B:GLU252 3.3 26.0 1.0
O B:HOH679 3.4 44.2 1.0
MG B:MG402 3.5 23.2 1.0
OD2 B:ASP251 3.5 27.8 1.0
CG B:GLU252 3.6 26.7 1.0
O3B B:PRP401 3.7 21.7 1.0
OD2 B:ASP111 3.9 36.1 1.0
OG1 B:THR115 4.1 32.2 1.0
O B:HOH667 4.3 39.7 1.0
O B:HOH503 4.3 18.4 1.0
O B:ASP251 4.5 25.9 1.0
OE1 B:GLU252 4.5 27.0 1.0
CG B:ASP111 4.6 34.7 1.0
O1B B:PRP401 4.6 25.7 1.0
CB B:ASP251 4.6 26.6 1.0
PB B:PRP401 4.7 23.6 1.0
C B:ASP251 4.7 26.6 1.0
O4 B:PRP401 4.8 34.0 1.0
OD1 B:ASP111 4.8 34.5 1.0
N B:ASP251 4.8 27.4 1.0
CA B:ASP251 4.9 27.1 1.0

Reference:

T.V.Cookson, A.Castell, E.M.Bulloch, G.L.Evans, F.L.Short, E.N.Baker, J.S.Lott, E.J.Parker. Alternative Substrates Reveal Catalytic Cycle and Key Binding Events in the Reaction Catalysed By Anthranilate Phosphoribosyltransferase From Mycobacterium Tuberculosis. Biochem.J. V. 461 87 2014.
ISSN: ISSN 0264-6021
PubMed: 24712732
DOI: 10.1042/BJ20140209
Page generated: Mon Aug 19 23:26:42 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy