Chlorine in PDB 3pug: Haloferax Volcanii Malate Synthase Native at 3MM Glyoxylate

All present enzymatic activity of Haloferax Volcanii Malate Synthase Native at 3MM Glyoxylate:
2.3.3.9;

The structure of Haloferax Volcanii Malate Synthase Native at 3MM Glyoxylate, PDB code: 3pug was solved by B.R.Howard, C.D.Bracken, A.M.Neighbor, G.C.Thomas, K.K.Lamlenn, H.L.Schubert, F.G.Whitby, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.70
Space group	H 3 2
Cell size a, b, c (Å), α, β, γ (°)	156.370, 156.370, 141.455, 90.00, 90.00, 120.00
R / Rfree (%)	19.8 / 26.3

The structure of Haloferax Volcanii Malate Synthase Native at 3MM Glyoxylate also contains other interesting chemical elements:

Magnesium	(Mg)	1 atom
Potassium	(K)	4 atoms

The binding sites of Chlorine atom in the Haloferax Volcanii Malate Synthase Native at 3MM Glyoxylate (pdb code 3pug). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Haloferax Volcanii Malate Synthase Native at 3MM Glyoxylate, PDB code: 3pug:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Haloferax Volcanii Malate Synthase Native at 3MM Glyoxylate


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Haloferax Volcanii Malate Synthase Native at 3MM Glyoxylate within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl701 b:45.7 occ:1.00 K A:K802 3.1 48.2 1.0 N A:ALA227 3.2 38.4 1.0 O A:HOH439 3.3 35.7 1.0 O A:GLY252 3.7 43.8 1.0 CA A:VAL226 3.8 37.5 1.0 NH2 A:ARG4 3.8 90.6 1.0 C A:VAL226 3.9 37.7 1.0 CB A:ALA227 4.0 36.7 1.0 O A:CYS225 4.0 39.6 1.0 CA A:ALA227 4.1 39.2 1.0 CB A:ALA220 4.1 38.0 1.0 CG1 A:VAL226 4.4 34.6 1.0 O A:ALA227 4.6 43.0 1.0 CZ A:ARG4 4.6 90.0 1.0 CB A:VAL226 4.6 37.3 1.0 NE A:ARG4 4.7 89.0 1.0 N A:VAL226 4.8 38.2 1.0 C A:CYS225 4.8 38.7 1.0 OG A:SER221 4.9 48.1 1.0 C A:ALA227 4.9 40.4 1.0 C A:GLY252 5.0 42.8 1.0

Chlorine binding site 2 out of 4 in the Haloferax Volcanii Malate Synthase Native at 3MM Glyoxylate


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Haloferax Volcanii Malate Synthase Native at 3MM Glyoxylate within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl702 b:49.3 occ:1.00 NH2 A:ARG95 3.2 32.1 1.0 NH1 A:ARG95 3.2 35.7 1.0 O A:ARG89 3.4 35.6 1.0 CD A:PRO92 3.5 37.6 1.0 CZ A:ARG95 3.6 36.9 1.0 C A:ASP90 3.7 40.5 1.0 N A:SER91 3.8 41.5 1.0 CA A:ASP90 3.9 40.0 1.0 O A:ASP90 4.1 42.1 1.0 CG A:PRO92 4.1 36.5 1.0 O A:HOH448 4.3 41.9 1.0 C A:ARG89 4.4 35.5 1.0 N A:PRO92 4.4 38.8 1.0 N A:ASP90 4.6 37.5 1.0 CA A:SER91 4.7 39.6 1.0 C A:SER91 4.8 40.0 1.0 NE A:ARG95 5.0 33.6 1.0

Chlorine binding site 3 out of 4 in the Haloferax Volcanii Malate Synthase Native at 3MM Glyoxylate


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Haloferax Volcanii Malate Synthase Native at 3MM Glyoxylate within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl703 b:73.9 occ:1.00 N A:ALA208 3.5 44.8 1.0 CA A:PRO207 3.7 47.1 1.0 O A:HOH482 3.8 61.1 1.0 CB A:PRO207 4.0 46.7 1.0 C A:PRO207 4.1 46.4 1.0 CB A:ALA208 4.2 40.1 1.0 CA A:ALA208 4.5 42.3 1.0

Chlorine binding site 4 out of 4 in the Haloferax Volcanii Malate Synthase Native at 3MM Glyoxylate


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Haloferax Volcanii Malate Synthase Native at 3MM Glyoxylate within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl704 b:81.4 occ:0.33 NH1 A:ARG218 3.6 42.9 1.0 NH2 A:ARG218 3.6 38.3 1.0 O A:HOH466 3.8 55.2 1.0 CZ A:ARG218 4.1 44.3 1.0 ND2 A:ASN215 4.2 40.2 1.0 OD1 A:ASN215 4.3 36.1 1.0 CG A:ASN215 4.5 36.3 1.0

C.D.Bracken, A.M.Neighbor, K.K.Lamlenn, G.C.Thomas, H.L.Schubert, F.G.Whitby, B.R.Howard. Crystal Structures of A Halophilic Archaeal Malate Synthase From Haloferax Volcanii and Comparisons with Isoforms A and G. Bmc Struct.Biol. V. 11 23 2011.
ISSN: ESSN 1472-6807
PubMed: 21569248
DOI: 10.1186/1472-6807-11-23