Chlorine in PDB 6mnz: Crystal Structure of Ribbx, A Two Domain 3,4-Dihydroxy-2-Butanone 4- Phosphate Synthase From A. Baumannii.

All present enzymatic activity of Crystal Structure of Ribbx, A Two Domain 3,4-Dihydroxy-2-Butanone 4- Phosphate Synthase From A. Baumannii.:
4.1.99.12;

The structure of Crystal Structure of Ribbx, A Two Domain 3,4-Dihydroxy-2-Butanone 4- Phosphate Synthase From A. Baumannii., PDB code: 6mnz was solved by J.Wang, G.Gonzalez-Gutierrez, D.P.Giedroc, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	68.43 / 2.66
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	116.707, 136.857, 51.856, 90.00, 98.53, 90.00
R / Rfree (%)	27.8 / 30.3

The binding sites of Chlorine atom in the Crystal Structure of Ribbx, A Two Domain 3,4-Dihydroxy-2-Butanone 4- Phosphate Synthase From A. Baumannii. (pdb code 6mnz). 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 Ribbx, A Two Domain 3,4-Dihydroxy-2-Butanone 4- Phosphate Synthase From A. Baumannii., PDB code: 6mnz:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of Ribbx, A Two Domain 3,4-Dihydroxy-2-Butanone 4- Phosphate Synthase From A. Baumannii.


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 Ribbx, A Two Domain 3,4-Dihydroxy-2-Butanone 4- Phosphate Synthase From A. Baumannii. within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl405 b:45.5 occ:1.00 HD1 A:HIS126 1.9 41.3 1.0 HB1 A:ALA91 2.6 42.1 1.0 HA2 A:GLY125 2.6 72.0 1.0 ND1 A:HIS126 2.7 34.4 1.0 HA3 A:GLY98 2.8 45.1 1.0 HB2 A:ALA91 2.8 42.1 1.0 HD12 A:ILE95 2.9 65.6 1.0 CB A:ALA91 3.2 35.1 1.0 H A:HIS126 3.2 52.1 1.0 CA A:GLY125 3.3 60.0 1.0 HA3 A:GLY125 3.3 72.0 1.0 O A:THR97 3.4 41.1 1.0 N A:HIS126 3.4 43.5 1.0 HE1 A:HIS126 3.5 50.4 1.0 CE1 A:HIS126 3.5 42.0 1.0 C A:GLY125 3.5 49.3 1.0 CA A:GLY98 3.7 37.6 1.0 CD1 A:ILE95 3.8 54.6 1.0 HB3 A:ALA91 3.8 42.1 1.0 HD11 A:ILE95 3.8 65.6 1.0 HB2 A:HIS126 3.9 48.1 1.0 CG A:HIS126 3.9 40.3 1.0 O A:HOH521 4.0 32.0 1.0 HA A:ALA91 4.1 46.4 1.0 HD13 A:ILE95 4.1 65.6 1.0 C A:THR97 4.2 43.3 1.0 HA2 A:GLY98 4.2 45.1 1.0 CB A:HIS126 4.2 40.1 1.0 CA A:ALA91 4.3 38.6 1.0 N A:GLY98 4.4 47.8 1.0 C A:GLY98 4.4 37.0 1.0 O A:GLY125 4.4 72.9 1.0 CA A:HIS126 4.5 38.9 1.0 O A:GLU90 4.5 38.1 1.0 O A:GLY98 4.5 30.9 1.0 N A:GLY125 4.6 41.1 1.0 O A:PRO124 4.6 39.4 1.0 HG1 A:THR107 4.7 45.5 1.0 NE2 A:HIS126 4.7 54.1 1.0 HG13 A:ILE95 4.9 57.0 1.0 CG1 A:ILE95 4.9 47.5 1.0 CD2 A:HIS126 4.9 36.8 1.0 HB A:ILE95 4.9 52.2 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of Ribbx, A Two Domain 3,4-Dihydroxy-2-Butanone 4- Phosphate Synthase From A. Baumannii.


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 Ribbx, A Two Domain 3,4-Dihydroxy-2-Butanone 4- Phosphate Synthase From A. Baumannii. within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl406 b:62.2 occ:1.00 HD1 B:HIS126 2.0 56.3 1.0 H B:HIS126 2.6 72.0 1.0 HB2 B:ALA91 2.7 60.2 1.0 HA3 B:GLY98 2.8 69.3 1.0 HA2 B:GLY125 2.8 72.2 1.0 HB1 B:ALA91 2.8 60.2 1.0 ND1 B:HIS126 2.9 46.9 1.0 N B:HIS126 3.0 60.0 1.0 HA3 B:GLY125 3.1 72.2 1.0 CB B:ALA91 3.1 50.2 1.0 CA B:GLY125 3.2 60.2 1.0 C B:GLY125 3.3 62.5 1.0 HA B:ALA91 3.4 46.7 1.0 HG21 B:ILE95 3.4 66.8 1.0 HB2 B:HIS126 3.4 47.4 1.0 CA B:GLY98 3.7 57.8 1.0 O B:GLU90 3.7 52.8 1.0 CG B:HIS126 3.8 45.4 1.0 CA B:ALA91 3.8 38.9 1.0 CE1 B:HIS126 3.8 51.9 1.0 CB B:HIS126 3.9 39.5 1.0 O B:THR97 3.9 55.9 1.0 HE1 B:HIS126 4.0 62.2 1.0 HB3 B:ALA91 4.0 60.2 1.0 CA B:HIS126 4.0 46.9 1.0 O B:GLY98 4.0 42.8 1.0 HA2 B:GLY98 4.1 69.3 1.0 C B:GLY98 4.2 55.1 1.0 CG2 B:ILE95 4.3 55.6 1.0 O B:GLY125 4.4 64.7 1.0 OG1 B:THR107 4.4 39.3 1.0 H B:ILE127 4.4 54.7 1.0 HG21 B:THR107 4.5 56.0 1.0 C B:GLU90 4.5 58.1 1.0 HG13 B:ILE95 4.6 61.1 1.0 N B:ALA91 4.6 53.3 1.0 C B:THR97 4.6 52.8 1.0 N B:GLY98 4.6 54.7 1.0 HG22 B:ILE95 4.6 66.8 1.0 N B:GLY125 4.6 47.8 1.0 HG23 B:ILE95 4.7 66.8 1.0 H B:ALA92 4.7 60.8 1.0 HA B:HIS126 4.7 56.2 1.0 HG1 B:THR107 4.8 47.1 1.0 HB3 B:HIS126 4.8 47.4 1.0 C B:HIS126 4.9 47.6 1.0 O B:PRO124 4.9 41.3 1.0 CD2 B:HIS126 4.9 49.8 1.0 NE2 B:HIS126 5.0 61.5 1.0 N B:ILE127 5.0 45.6 1.0

J.Wang, Z.R.Lonergan, G.Gonzalez-Gutierrez, B.L.Nairn, C.N.Maxwell, Y.Zhang, C.Andreini, J.A.Karty, W.J.Chazin, J.C.Trinidad, E.P.Skaar, D.P.Giedroc. Multi-Metal Restriction By Calprotectin Impacts De Novo Flavin Biosynthesis in Acinetobacter Baumannii. Cell Chem Biol V. 26 745 2019.
ISSN: ESSN 2451-9456
PubMed: 30905682
DOI: 10.1016/J.CHEMBIOL.2019.02.011