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Arsenic in PDB 4wb0: Crystal Structure of the Broad Specificity Aminotransferase From Leishmania Mexicana

Protein crystallography data

The structure of Crystal Structure of the Broad Specificity Aminotransferase From Leishmania Mexicana, PDB code: 4wb0 was solved by J.Wen, C.Nowicki, W.Blankenfeldt, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 76.38 / 1.91
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 86.418, 90.564, 142.159, 90.00, 90.00, 90.00
R / Rfree (%) 17.7 / 21

Arsenic Binding Sites:

The binding sites of Arsenic atom in the Crystal Structure of the Broad Specificity Aminotransferase From Leishmania Mexicana (pdb code 4wb0). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total 2 binding sites of Arsenic where determined in the Crystal Structure of the Broad Specificity Aminotransferase From Leishmania Mexicana, PDB code: 4wb0:
Jump to Arsenic binding site number: 1; 2;

Arsenic binding site 1 out of 2 in 4wb0

Go back to Arsenic Binding Sites List in 4wb0
Arsenic binding site 1 out of 2 in the Crystal Structure of the Broad Specificity Aminotransferase From Leishmania Mexicana


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of Crystal Structure of the Broad Specificity Aminotransferase From Leishmania Mexicana within 5.0Å range:
probe atom residue distance (Å) B Occ
A:As501

b:47.7
occ:0.96
AS A:CAC501 0.0 47.7 1.0
O2 A:CAC501 1.7 28.1 1.0
O1 A:CAC501 1.8 26.8 1.0
C1 A:CAC501 2.0 57.1 1.0
C2 A:CAC501 2.0 0.5 1.0
H11 A:CAC501 2.5 68.5 1.0
H13 A:CAC501 2.5 68.5 1.0
H12 A:CAC501 2.5 68.5 1.0
H23 A:CAC501 2.5 0.8 1.0
H21 A:CAC501 2.5 0.8 1.0
H22 A:CAC501 2.5 0.8 1.0
HH B:TYR75 2.9 35.7 1.0
HH22 A:ARG265 3.0 29.8 1.0
HG1 A:THR111 3.0 35.8 1.0
HH12 A:ARG265 3.2 27.5 1.0
HG A:SER256 3.2 28.5 1.0
HG A:SER109 3.2 35.0 1.0
H A:THR111 3.3 28.5 1.0
HB3 A:SER109 3.6 34.2 1.0
H A:GLY110 3.6 26.9 1.0
OH B:TYR75 3.7 29.8 1.0
OG A:SER109 3.7 29.2 1.0
OG1 A:THR111 3.8 29.8 1.0
NH2 A:ARG265 3.8 24.9 1.0
HE1 B:TYR75 3.9 35.2 1.0
OG A:SER256 4.0 23.8 1.0
NH1 A:ARG265 4.0 22.9 1.0
N A:THR111 4.1 23.8 1.0
CB A:SER109 4.1 28.5 1.0
N A:GLY110 4.2 22.4 1.0
OG A:SER254 4.2 21.8 1.0
HA3 A:GLY110 4.2 27.0 1.0
HB2 A:SER256 4.3 25.2 1.0
HE3 A:LYS257 4.4 52.7 1.0
CZ A:ARG265 4.4 23.2 1.0
HH21 A:ARG265 4.4 29.8 1.0
HB2 A:SER254 4.5 24.5 1.0
CE1 B:TYR75 4.5 29.3 1.0
CZ B:TYR75 4.5 31.9 1.0
HH2 A:TRP139 4.6 68.4 1.0
HE2 A:LYS257 4.6 52.7 1.0
HB A:THR111 4.6 33.9 1.0
CB A:SER256 4.6 21.0 1.0
CA A:GLY110 4.6 22.5 1.0
HB2 A:SER109 4.7 34.2 1.0
CB A:THR111 4.7 28.2 1.0
HH11 A:ARG265 4.7 27.5 1.0
C A:GLY110 4.9 21.9 1.0
HB B:THR295 4.9 38.4 1.0
HB3 A:SER256 4.9 25.2 1.0
HG A:SER254 4.9 26.1 1.0
CB A:SER254 4.9 20.4 1.0
CE A:LYS257 5.0 43.9 1.0

Arsenic binding site 2 out of 2 in 4wb0

Go back to Arsenic Binding Sites List in 4wb0
Arsenic binding site 2 out of 2 in the Crystal Structure of the Broad Specificity Aminotransferase From Leishmania Mexicana


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 2 of Crystal Structure of the Broad Specificity Aminotransferase From Leishmania Mexicana within 5.0Å range:
probe atom residue distance (Å) B Occ
B:As501

b:49.5
occ:0.92
AS B:CAC501 0.0 49.5 0.9
O2 B:CAC501 1.8 29.5 0.9
O1 B:CAC501 1.8 26.8 0.9
C1 B:CAC501 2.0 0.4 0.9
C2 B:CAC501 2.0 63.2 0.9
H11 B:CAC501 2.5 0.5 0.9
H13 B:CAC501 2.5 0.5 0.9
H12 B:CAC501 2.5 0.5 0.9
H21 B:CAC501 2.5 75.9 0.9
H22 B:CAC501 2.5 75.9 0.9
H23 B:CAC501 2.5 75.9 0.9
HH A:TYR75 3.0 40.8 1.0
HH22 B:ARG265 3.0 31.7 1.0
HG1 B:THR111 3.0 37.4 1.0
HG B:SER256 3.2 28.5 1.0
HH12 B:ARG265 3.2 32.7 1.0
HZ1 B:LYS257 3.3 42.1 0.7
HG B:SER109 3.4 39.3 1.0
H B:THR111 3.4 32.2 1.0
H B:GLY110 3.4 31.1 1.0
HB3 B:SER109 3.4 37.2 1.0
HG B:SER254 3.5 29.7 1.0
OH A:TYR75 3.7 34.0 1.0
OG B:SER109 3.7 32.7 1.0
OG1 B:THR111 3.8 31.1 1.0
NH2 B:ARG265 3.8 26.4 1.0
HZ3 B:LYS257 3.8 42.1 0.7
OG B:SER256 3.9 23.8 1.0
HE1 A:TYR75 3.9 34.0 1.0
NH1 B:ARG265 4.0 27.3 1.0
NZ B:LYS257 4.0 35.1 0.7
HB2 B:SER256 4.0 29.8 1.0
OG B:SER254 4.1 24.8 1.0
N B:GLY110 4.1 25.9 1.0
CB B:SER109 4.1 31.0 1.0
HA3 B:GLY110 4.1 31.4 1.0
N B:THR111 4.1 26.8 1.0
HB2 B:SER254 4.3 31.9 1.0
HZ2 B:LYS257 4.3 42.1 0.7
HE2 B:LYS257 4.4 42.9 0.3
CZ B:ARG265 4.4 26.0 1.0
CB B:SER256 4.4 24.8 1.0
HH21 B:ARG265 4.5 31.7 1.0
CA B:GLY110 4.5 26.1 1.0
CE1 A:TYR75 4.6 28.3 1.0
HG21 A:THR295 4.6 39.4 1.0
CZ A:TYR75 4.6 30.5 1.0
HG1 A:THR295 4.6 37.3 1.0
HB2 B:SER109 4.6 37.2 1.0
HH11 B:ARG265 4.7 32.7 1.0
HB3 B:SER256 4.7 29.8 1.0
HB B:THR111 4.7 34.5 1.0
CB B:SER254 4.7 26.6 1.0
CB B:THR111 4.7 28.8 1.0
HH2 B:TRP139 4.8 50.7 1.0
HB A:THR295 4.8 35.4 1.0
C B:GLY110 4.8 26.1 1.0
CA B:THR111 5.0 26.6 1.0

Reference:

J.Wen, C.Nowicki, W.Blankenfeldt. Structural Basis For the Relaxed Substrate Selectivity of Leishmania Mexicana Broad Specificity Aminotransferase. Mol.Biochem.Parasitol. V. 202 34 2015.
ISSN: ISSN 0166-6851
PubMed: 26456583
DOI: 10.1016/J.MOLBIOPARA.2015.09.007
Page generated: Mon Jul 7 00:06:48 2025

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