Nickel in PDB 7w58: Crystal Structure of Acyl-Carrier Protein Synthase From Mycobacterium Smegmatis

All present enzymatic activity of Crystal Structure of Acyl-Carrier Protein Synthase From Mycobacterium Smegmatis:
2.7.8.7;

The structure of Crystal Structure of Acyl-Carrier Protein Synthase From Mycobacterium Smegmatis, PDB code: 7w58 was solved by S.Yadav, I.Bhatia, B.K.Biswal, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.63 / 2.27
Space group	H 3
Cell size a, b, c (Å), α, β, γ (°)	67.64, 67.64, 85.779, 90, 90, 120
R / Rfree (%)	16.7 / 20.3

The binding sites of Nickel atom in the Crystal Structure of Acyl-Carrier Protein Synthase From Mycobacterium Smegmatis (pdb code 7w58). This binding sites where shown within 5.0 Angstroms radius around Nickel atom.
In total only one binding site of Nickel was determined in the Crystal Structure of Acyl-Carrier Protein Synthase From Mycobacterium Smegmatis, PDB code: 7w58:

Nickel binding site 1 out of 1 in the Crystal Structure of Acyl-Carrier Protein Synthase From Mycobacterium Smegmatis


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of Crystal Structure of Acyl-Carrier Protein Synthase From Mycobacterium Smegmatis within 5.0Å range: probe atom residue distance (Å) B Occ A:Ni203 b:49.7 occ:1.00 NE2 A:HIS116 2.0 25.4 1.0 NE2 A:HIS49 2.2 43.6 1.0 O A:HOH371 2.3 51.9 1.0 O A:HOH385 2.6 42.2 1.0 CE1 A:HIS116 3.0 23.9 1.0 O A:HOH384 3.0 55.3 1.0 CD2 A:HIS116 3.1 24.1 1.0 CD2 A:HIS49 3.1 39.8 1.0 CE1 A:HIS49 3.1 42.6 1.0 O A:HOH392 3.4 45.1 1.0 ND1 A:HIS116 4.1 23.6 1.0 CG A:HIS116 4.2 24.6 1.0 CG A:HIS49 4.2 36.9 1.0 ND1 A:HIS49 4.2 40.2 1.0 O A:HOH327 4.4 40.1 1.0 O A:HOH374 4.8 37.4 1.0

I.Bhatia, S.Yadav, B.K.Biswal. Identification, Structure Determination and Analysis of Mycobacterium Smegmatis Acyl-Carrier Protein Synthase (Acps) Crystallized Serendipitously. Acta Crystallogr.,Sect.F V. 78 252 2022.
ISSN: ESSN 2053-230X
PubMed: 35787552
DOI: 10.1107/S2053230X22005738