Zinc in PDB 3fig: Crystal Structure of Leucine-Bound Leua From Mycobacterium Tuberculosis

All present enzymatic activity of Crystal Structure of Leucine-Bound Leua From Mycobacterium Tuberculosis:
2.3.3.13;

The structure of Crystal Structure of Leucine-Bound Leua From Mycobacterium Tuberculosis, PDB code: 3fig was solved by N.Koon, C.J.Squire, E.N.Baker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	27.66 / 2.30
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	54.207, 154.258, 68.669, 90.00, 97.99, 90.00
R / Rfree (%)	16.6 / 24.4

The binding sites of Zinc atom in the Crystal Structure of Leucine-Bound Leua From Mycobacterium Tuberculosis (pdb code 3fig). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of Leucine-Bound Leua From Mycobacterium Tuberculosis, PDB code: 3fig:

Zinc binding site 1 out of 1 in the Crystal Structure of Leucine-Bound Leua From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Leucine-Bound Leua From Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn645 b:30.0 occ:0.30 OD2 B:ASP81 2.1 39.3 1.0 NE2 B:HIS287 2.2 28.4 1.0 NE2 B:HIS285 2.4 25.9 1.0 CE1 B:HIS287 2.8 36.6 1.0 CG B:ASP81 3.1 36.1 1.0 CD2 B:HIS285 3.1 23.4 1.0 O B:HOH712 3.3 31.3 1.0 CE1 B:HIS285 3.3 21.2 1.0 OD1 B:ASP81 3.4 42.4 1.0 CD2 B:HIS287 3.4 28.1 1.0 OD1 B:ASN321 3.7 32.5 1.0 ND1 B:HIS287 4.1 34.3 1.0 O B:HOH783 4.2 27.8 1.0 CG B:HIS285 4.3 24.9 1.0 ND1 B:HIS285 4.3 23.0 1.0 NH2 B:ARG80 4.4 28.0 1.0 CG B:HIS287 4.4 23.8 1.0 CB B:ASP81 4.5 28.4 1.0 CG B:ASN321 4.6 24.4 1.0 ND2 B:ASN321 4.9 18.6 1.0

N.Koon, C.J.Squire, E.N.Baker. Crystal Structure of Leua From Mycobacterium Tuberculosis, A Key Enzyme in Leucine Biosynthesis. Proc.Natl.Acad.Sci.Usa V. 101 8295 2004.
ISSN: ISSN 0027-8424
PubMed: 15159544
DOI: 10.1073/PNAS.0400820101