Chlorine in PDB 3af1: Pantothenate Kinase From Mycobacterium Tuberculosis (Mtpank) in Complex with Gdp

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

The structure of Pantothenate Kinase From Mycobacterium Tuberculosis (Mtpank) in Complex with Gdp, PDB code: 3af1 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)	34.06 / 2.50
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	103.900, 103.900, 90.210, 90.00, 90.00, 120.00
R / Rfree (%)	19.3 / 24.3

The binding sites of Chlorine atom in the Pantothenate Kinase From Mycobacterium Tuberculosis (Mtpank) in Complex with Gdp (pdb code 3af1). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Pantothenate Kinase From Mycobacterium Tuberculosis (Mtpank) in Complex with Gdp, PDB code: 3af1:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Pantothenate Kinase From Mycobacterium Tuberculosis (Mtpank) in Complex with Gdp


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 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl315 b:82.1 occ:1.00 NE A:ARG270 3.5 63.9 1.0 O A:HOH379 3.8 51.6 1.0 OE1 A:GLN233 3.8 54.5 1.0 NH2 A:ARG270 3.9 68.8 1.0 OE1 A:GLU232 4.0 48.7 1.0 CD A:GLU232 4.2 43.4 1.0 CZ A:ARG270 4.2 69.0 1.0 CG2 A:VAL236 4.2 30.5 1.0 CG A:GLU232 4.3 36.4 1.0 CD A:ARG270 4.5 57.5 1.0 CG A:ARG270 4.6 50.0 1.0 O A:HOH459 4.6 59.3 1.0 CB A:VAL236 4.7 35.3 1.0 CD A:GLN233 4.8 49.5 1.0 CA A:GLN233 4.8 35.7 1.0 OE2 A:GLU232 4.9 42.6 1.0 CG1 A:VAL236 4.9 34.2 1.0 N A:GLN233 4.9 35.5 1.0

Chlorine binding site 2 out of 3 in the Pantothenate Kinase From Mycobacterium Tuberculosis (Mtpank) in Complex with Gdp


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Pantothenate Kinase From Mycobacterium Tuberculosis (Mtpank) in Complex with Gdp within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl316 b:58.6 occ:1.00 N A:ASN204 2.9 37.8 1.0 CB A:ASN204 3.2 42.1 1.0 CA A:ASN204 3.3 39.1 1.0 OG1 A:THR128 3.4 32.2 1.0 C A:ASN204 3.6 36.3 1.0 N A:VAL205 3.8 34.0 1.0 CZ A:TYR153 3.8 39.2 1.0 CE1 A:TYR153 3.9 36.3 1.0 CB A:THR128 4.0 28.6 1.0 C A:LEU203 4.0 35.9 1.0 N A:LEU203 4.0 31.8 1.0 OH A:TYR153 4.1 36.5 1.0 CG2 A:THR128 4.1 23.7 1.0 CL A:CL317 4.1 96.1 1.0 C A:GLY202 4.2 29.1 1.0 CE2 A:TYR153 4.2 38.8 1.0 ND2 A:ASN204 4.2 48.3 1.0 CG A:ASN204 4.2 50.4 1.0 CD1 A:TYR153 4.3 35.1 1.0 CG1 A:VAL205 4.3 31.1 1.0 CA A:LEU203 4.3 33.7 1.0 CB A:LEU203 4.3 33.6 1.0 O A:ASN204 4.4 35.8 1.0 CA A:GLY202 4.4 26.8 1.0 O A:HOH358 4.4 36.1 1.0 CA A:VAL205 4.5 31.1 1.0 CD2 A:TYR153 4.6 37.0 1.0 CG A:TYR153 4.7 37.4 1.0 O A:GLY202 4.7 31.6 1.0

Chlorine binding site 3 out of 3 in the Pantothenate Kinase From Mycobacterium Tuberculosis (Mtpank) in Complex with Gdp


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Pantothenate Kinase From Mycobacterium Tuberculosis (Mtpank) in Complex with Gdp within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl317 b:96.1 occ:1.00 O A:HOH395 2.8 39.9 1.0 NE2 A:GLN207 3.3 70.3 1.0 CG A:ARG155 3.7 50.4 1.0 CD A:ARG155 3.7 59.1 1.0 CB A:ASN204 3.8 42.1 1.0 O A:ASN204 3.9 35.8 1.0 CL A:CL316 4.1 58.6 1.0 C A:ASN204 4.4 36.3 1.0 CD A:GLN207 4.5 68.2 1.0 CE A:MET213 4.5 41.2 1.0 CA A:PRO150 4.7 35.0 1.0 O A:PRO150 4.7 37.4 1.0 CA A:ASN204 4.7 39.1 1.0 CB A:GLN207 4.7 39.1 1.0 CD1 A:TYR153 4.8 35.1 1.0 CB A:PRO150 4.9 33.0 1.0 CG A:ASN204 4.9 50.4 1.0 NE A:ARG155 4.9 63.2 1.0 CB A:TYR153 4.9 34.0 1.0 CD2 A:LEU158 4.9 30.1 1.0 CG A:GLN207 4.9 50.6 1.0 CG A:TYR153 5.0 37.4 1.0 CB A:ARG155 5.0 39.3 1.0

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