Chlorine in PDB 6p90: Crystal Structure of PADHDPS2-H56Q Mutant

All present enzymatic activity of Crystal Structure of PADHDPS2-H56Q Mutant:
4.3.3.7;

The structure of Crystal Structure of PADHDPS2-H56Q Mutant, PDB code: 6p90 was solved by R.E.Impey, S.Panjikar, C.J.Hall, L.J.Bock, J.M.Sutton, M.A.Perugini, T.P.Soares Da Costa, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	43.181, 123.338, 57.418, 90.00, 107.57, 90.00
R / Rfree (%)	18.6 / 21.9

The binding sites of Chlorine atom in the Crystal Structure of PADHDPS2-H56Q Mutant (pdb code 6p90). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of PADHDPS2-H56Q Mutant, PDB code: 6p90:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of PADHDPS2-H56Q Mutant


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of PADHDPS2-H56Q Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl302 b:40.6 occ:1.00 O B:HOH526 2.9 37.0 1.0 N B:ASN248 3.2 21.7 1.0 NZ A:LYS109 3.4 52.7 1.0 CA B:SER247 3.6 27.8 1.0 CD2 B:PHE244 3.7 34.4 1.0 NH2 B:ARG138 3.7 34.2 1.0 CB B:ASN248 3.8 21.4 1.0 C B:SER247 3.9 23.6 1.0 CE A:LYS109 4.1 54.8 1.0 CA B:ASN248 4.2 21.5 1.0 CB B:SER247 4.2 30.0 1.0 CE2 B:PHE244 4.3 34.0 1.0 OG B:SER247 4.4 41.3 1.0 O B:GLU246 4.5 27.1 1.0 O B:HOH532 4.6 28.2 1.0 CZ B:ARG138 4.6 34.2 1.0 CG B:PHE244 4.7 31.4 1.0 N B:SER247 4.7 25.9 1.0 O B:ASN248 4.7 26.9 1.0 CB B:PHE244 4.8 27.3 1.0 C B:ASN248 5.0 23.9 1.0 C B:GLU246 5.0 29.4 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of PADHDPS2-H56Q Mutant


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of PADHDPS2-H56Q Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl303 b:40.2 occ:1.00 O A:HOH457 3.2 34.2 1.0 N A:ASN248 3.3 24.3 1.0 NZ B:LYS109 3.4 47.1 1.0 CD1 A:PHE244 3.7 38.0 1.0 NH2 A:ARG138 3.7 36.5 1.0 CA A:SER247 3.7 27.2 1.0 CB A:ASN248 3.9 24.9 1.0 CE B:LYS109 4.0 46.6 1.0 C A:SER247 4.0 26.8 1.0 CA A:ASN248 4.2 24.1 1.0 CE1 A:PHE244 4.3 34.3 1.0 CB A:SER247 4.3 25.9 1.0 CZ A:ARG138 4.6 38.1 1.0 CG A:PHE244 4.7 37.8 1.0 O A:GLU246 4.7 25.6 1.0 OG A:SER247 4.8 30.3 1.0 CB A:PHE244 4.8 30.8 1.0 N A:SER247 4.8 25.8 1.0 O A:ASN248 4.8 26.5 1.0

R.E.Impey, S.Panjikar, C.J.Hall, L.J.Bock, J.M.Sutton, M.A.Perugini, T.P.Soares Da Costa. Identification of Two Dihydrodipicolinate Synthase Isoforms From Pseudomonas Aeruginosa That Differ in Allosteric Regulation. Febs J. 2019.
ISSN: ISSN 1742-464X
PubMed: 31330085
DOI: 10.1111/FEBS.15014