Bromine in PDB 6ny7: Crystal Structure of Ndm-1 D199N with Compound 16

All present enzymatic activity of Crystal Structure of Ndm-1 D199N with Compound 16:
3.5.2.6;

The structure of Crystal Structure of Ndm-1 D199N with Compound 16, PDB code: 6ny7 was solved by A.Akhtar, Y.Chen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.07 / 1.40
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	41.571, 59.774, 42.531, 90.00, 97.88, 90.00
R / Rfree (%)	14.4 / 17.5

The structure of Crystal Structure of Ndm-1 D199N with Compound 16 also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Bromine atom in the Crystal Structure of Ndm-1 D199N with Compound 16 (pdb code 6ny7). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 2 binding sites of Bromine where determined in the Crystal Structure of Ndm-1 D199N with Compound 16, PDB code: 6ny7:
Jump to Bromine binding site number: 1; 2;

Bromine binding site 1 out of 2 in the Crystal Structure of Ndm-1 D199N with Compound 16


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Crystal Structure of Ndm-1 D199N with Compound 16 within 5.0Å range: probe atom residue distance (Å) B Occ A:Br303 b:49.7 occ:0.75 BR01 A:L8J303 0.0 49.7 0.8 C02 A:L8J303 1.9 46.2 0.8 C03 A:L8J303 2.8 44.1 0.8 C06 A:L8J303 2.9 43.9 0.8 O A:HOH599 3.9 31.9 1.0 CB A:PHE70 4.1 40.1 1.0 C04 A:L8J303 4.1 41.6 0.8 C07 A:L8J303 4.2 41.4 0.8 CG2 A:VAL73 4.3 16.4 1.0 O A:HOH638 4.4 36.5 1.0 O A:PHE70 4.5 36.2 1.0 O A:HOH682 4.6 45.1 1.0 CD1 A:PHE70 4.7 43.2 1.0 CG A:PHE70 4.7 42.2 1.0 C A:PHE70 4.7 34.9 1.0 C08 A:L8J303 4.8 38.6 0.8 CA A:PHE70 4.9 38.1 1.0

Bromine binding site 2 out of 2 in the Crystal Structure of Ndm-1 D199N with Compound 16


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Crystal Structure of Ndm-1 D199N with Compound 16 within 5.0Å range: probe atom residue distance (Å) B Occ A:Br303 b:41.4 occ:0.75 BR05 A:L8J303 0.0 41.4 0.8 C04 A:L8J303 1.9 41.6 0.8 C03 A:L8J303 2.9 44.1 0.8 C08 A:L8J303 2.9 38.6 0.8 C10 A:L8J303 3.0 24.4 0.8 C09 A:L8J303 3.2 33.3 0.8 O13 A:L8J303 3.3 18.9 0.8 O A:HOH667 3.4 33.2 1.0 O A:HOH453 3.5 21.6 1.0 CG1 A:VAL73 3.5 14.7 1.0 O A:HOH643 3.6 32.1 1.0 CG A:HIS250 3.6 12.4 1.0 O A:HOH427 3.6 23.3 1.0 CD2 A:HIS250 3.6 13.0 1.0 ND1 A:HIS250 3.7 12.0 1.0 NE2 A:HIS250 3.7 12.7 1.0 P11 A:L8J303 3.7 16.4 0.8 CE1 A:HIS250 3.8 11.6 1.0 O A:HOH655 4.0 31.1 1.0 C02 A:L8J303 4.1 46.2 0.8 C07 A:L8J303 4.1 41.4 0.8 CB A:HIS250 4.2 13.5 1.0 O12 A:L8J303 4.6 15.4 0.8 C15 A:L8J303 4.6 37.8 0.8 C06 A:L8J303 4.6 43.9 0.8 O A:HOH572 4.8 32.8 1.0 CB A:VAL73 4.9 13.7 1.0 O14 A:L8J303 4.9 17.3 0.8 CG2 A:VAL73 5.0 16.4 1.0

O.A.Pemberton, P.Jaishankar, A.Akhtar, J.L.Adams, L.N.Shaw, A.R.Renslo, Y.Chen. Heteroaryl Phosphonates As Noncovalent Inhibitors of Both Serine- and Metallocarbapenemases. J.Med.Chem. V. 62 8480 2019.
ISSN: ISSN 0022-2623
PubMed: 31483651
DOI: 10.1021/ACS.JMEDCHEM.9B00728