Chlorine in PDB 3mla: Banadd in Complex with Inhibitor 1_02

All present enzymatic activity of Banadd in Complex with Inhibitor 1_02:
2.7.7.18;

The structure of Banadd in Complex with Inhibitor 1_02, PDB code: 3mla was solved by N.Huang, Y.Eyobo, H.Zhang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.71 / 1.75
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	88.586, 97.498, 44.280, 90.00, 90.00, 90.00
R / Rfree (%)	18.9 / 23

The binding sites of Chlorine atom in the Banadd in Complex with Inhibitor 1_02 (pdb code 3mla). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Banadd in Complex with Inhibitor 1_02, PDB code: 3mla:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Banadd in Complex with Inhibitor 1_02


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Banadd in Complex with Inhibitor 1_02 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl190 b:35.8 occ:0.53 CLAF A:JJZ190 0.0 35.8 0.5 CAG A:JJZ190 1.7 28.8 0.5 CAA A:JJZ190 2.7 33.2 0.5 CAH A:JJZ190 2.7 19.2 0.5 O A:HOH345 3.0 46.0 1.0 CG2 A:VAL131 3.0 34.9 1.0 N A:GLY106 3.3 23.1 1.0 CA A:GLY106 3.3 25.7 1.0 C A:ILE105 3.5 18.3 1.0 O A:ILE105 3.7 20.5 1.0 CAB A:JJZ190 4.0 34.3 0.5 CAI A:JJZ190 4.0 23.8 0.5 CD1 A:ILE21 4.0 31.3 1.0 CG2 A:ILE104 4.2 19.2 1.0 CG2 A:ILE21 4.3 22.2 1.0 CB A:VAL131 4.3 34.6 1.0 CA A:ILE105 4.3 17.6 1.0 CAC A:JJZ190 4.5 34.3 0.5 CG1 A:VAL131 4.5 37.6 1.0 O A:HOH350 4.7 47.7 1.0 N A:ILE105 4.7 16.1 1.0 C A:GLY106 4.7 25.9 1.0 CG1 A:ILE21 4.9 23.7 1.0

Chlorine binding site 2 out of 2 in the Banadd in Complex with Inhibitor 1_02


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Banadd in Complex with Inhibitor 1_02 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl190 b:0.2 occ:0.47 CLAF A:JJZ190 0.0 0.2 0.5 CAG A:JJZ190 1.7 33.4 0.5 CAA A:JJZ190 2.7 35.6 0.5 CAH A:JJZ190 2.7 29.3 0.5 ND1 B:HIS18 2.9 29.2 1.0 O B:HOH285 3.1 45.7 1.0 CD1 B:ILE7 3.2 21.6 1.0 O B:HOH319 3.4 29.1 1.0 CD1 B:ILE21 3.7 26.9 1.0 CE1 B:HIS18 3.8 21.0 1.0 CA B:HIS18 3.9 21.0 1.0 CG B:HIS18 3.9 19.1 1.0 CG1 B:ILE7 3.9 20.9 1.0 CAB A:JJZ190 4.0 37.7 0.5 CAI A:JJZ190 4.0 25.5 0.5 CB B:HIS18 4.1 19.0 1.0 O B:HOH265 4.2 50.4 1.0 CAC A:JJZ190 4.5 29.8 0.5 CB B:ILE21 4.7 16.9 1.0 N B:HIS18 4.7 16.7 1.0 CG1 B:ILE21 4.8 19.3 1.0 O B:HIS18 4.8 19.8 1.0 CG2 B:ILE21 4.8 22.6 1.0 O B:GLY17 4.9 18.9 1.0 C B:HIS18 4.9 22.7 1.0 NE2 B:HIS18 4.9 24.5 1.0 CE2 B:PHE11 5.0 24.6 1.0

N.Huang, R.Kolhatkar, Y.Eyobo, L.Sorci, I.Rodionova, A.L.Osterman, A.D.Mackerell, H.Zhang. Complexes of Bacterial Nicotinate Mononucleotide Adenylyltransferase with Inhibitors: Implication For Structure-Based Drug Design and Improvement. J.Med.Chem. V. 53 5229 2010.
ISSN: ISSN 0022-2623
PubMed: 20578699
DOI: 10.1021/JM100377F