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Chlorine in PDB 3af0: Pantothenate Kinase From Mycobacterium Tuberculosis (Mtpank) in Complex with Gdp and Pantothenate

Enzymatic activity of Pantothenate Kinase From Mycobacterium Tuberculosis (Mtpank) in Complex with Gdp and Pantothenate

All present enzymatic activity of Pantothenate Kinase From Mycobacterium Tuberculosis (Mtpank) in Complex with Gdp and Pantothenate:
2.7.1.33;

Protein crystallography data

The structure of Pantothenate Kinase From Mycobacterium Tuberculosis (Mtpank) in Complex with Gdp and Pantothenate, PDB code: 3af0 was solved by B.Chetnani, P.Kumar, A.Surolia, M.Vijayan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 34.28 / 2.50
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 104.730, 104.730, 90.400, 90.00, 90.00, 120.00
R / Rfree (%) 20.7 / 25.4

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Pantothenate Kinase From Mycobacterium Tuberculosis (Mtpank) in Complex with Gdp and Pantothenate (pdb code 3af0). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Pantothenate Kinase From Mycobacterium Tuberculosis (Mtpank) in Complex with Gdp and Pantothenate, PDB code: 3af0:

Chlorine binding site 1 out of 1 in 3af0

Go back to Chlorine Binding Sites List in 3af0
Chlorine binding site 1 out of 1 in the Pantothenate Kinase From Mycobacterium Tuberculosis (Mtpank) in Complex with Gdp and Pantothenate


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Pantothenate Kinase From Mycobacterium Tuberculosis (Mtpank) in Complex with Gdp and Pantothenate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl315

b:66.0
occ:1.00
 N A:ASN204 3.0 41.6 1.0
OG1 A:THR128 3.4 40.1 1.0
CA A:ASN204 3.5 43.5 1.0
CB A:ASN204 3.5 45.4 1.0
C A:ASN204 3.7 43.4 1.0
N A:VAL205 3.7 40.1 1.0
N A:LEU203 3.9 34.6 1.0
CB A:THR128 3.9 32.9 1.0
CZ A:TYR153 4.0 42.2 1.0
CG2 A:THR128 4.1 28.9 1.0
C A:LEU203 4.1 38.5 1.0
CE2 A:TYR153 4.1 40.3 1.0
C A:GLY202 4.1 33.1 1.0
CG1 A:VAL205 4.2 36.5 1.0
OH A:TYR153 4.3 40.5 1.0
CE1 A:TYR153 4.3 39.4 1.0
CA A:GLY202 4.3 32.8 1.0
CA A:LEU203 4.3 36.1 1.0
O A:ASN204 4.4 45.6 1.0
CD2 A:TYR153 4.5 37.2 1.0
CB A:LEU203 4.5 35.4 1.0
CA A:VAL205 4.5 37.6 1.0
O A:HOH360 4.7 43.3 1.0
CD1 A:TYR153 4.7 38.7 1.0
CG A:ASN204 4.8 46.7 1.0
O A:GLY202 4.8 37.7 1.0
CG A:TYR153 4.8 40.9 1.0
O A:HOH372 4.8 53.3 1.0
ND2 A:ASN204 5.0 41.8 1.0
CB A:VAL205 5.0 37.1 1.0

Reference:

B.Chetnani, P.Kumar, A.Surolia, M.Vijayan. M. Tuberculosis Pantothenate Kinase: Dual Substrate Specificity and Unusual Changes in Ligand Locations J.Mol.Biol. V. 400 171 2010.
ISSN: ISSN 0022-2836
PubMed: 20451532
DOI: 10.1016/J.JMB.2010.04.064
Page generated: Fri Jul 11 03:04:48 2025

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