Zinc in PDB 6l2m: The Structure of the Trna-Specific Deaminase Mutant From M. Capricolum

The structure of The Structure of the Trna-Specific Deaminase Mutant From M. Capricolum, PDB code: 6l2m was solved by W.Xie, H.Liu, S.Wu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.14 / 2.30
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	55.589, 55.589, 109.227, 90.00, 90.00, 120.00
R / Rfree (%)	19.8 / 25.1

The structure of The Structure of the Trna-Specific Deaminase Mutant From M. Capricolum also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Zinc atom in the The Structure of the Trna-Specific Deaminase Mutant From M. Capricolum (pdb code 6l2m). 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 The Structure of the Trna-Specific Deaminase Mutant From M. Capricolum, PDB code: 6l2m:

Zinc binding site 1 out of 1 in the The Structure of the Trna-Specific Deaminase Mutant From M. Capricolum


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Structure of the Trna-Specific Deaminase Mutant From M. Capricolum within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn201 b:31.3 occ:1.00 ND1 A:HIS54 2.1 34.4 1.0 O A:HOH302 2.2 27.1 1.0 SG A:CYS87 2.4 30.2 1.0 SG A:CYS84 2.4 33.1 1.0 CE1 A:HIS54 3.0 31.7 1.0 CG A:HIS54 3.1 36.5 1.0 CB A:CYS87 3.3 30.1 1.0 CB A:CYS84 3.4 29.8 1.0 CB A:HIS54 3.4 35.4 1.0 N A:CYS84 3.8 31.9 1.0 CE A:MET86 3.9 27.6 1.0 N A:CYS87 4.0 26.9 1.0 OE2 A:GLU56 4.0 36.0 1.0 CA A:CYS84 4.1 30.1 1.0 NE2 A:HIS54 4.1 34.3 1.0 CD2 A:HIS54 4.2 32.0 1.0 CA A:CYS87 4.2 23.4 1.0 O A:HOH332 4.3 42.7 1.0 C A:CYS84 4.6 33.2 1.0 O A:CYS84 4.6 29.9 1.0 CB A:MET86 4.9 26.2 1.0 C A:PRO83 4.9 32.9 1.0 CD A:GLU56 4.9 30.9 1.0 CA A:HIS54 5.0 27.4 1.0

H.Liu, S.Wu, D.Ran, W.Xie. Structure of A Trna-Specific Deaminase with Compromised Deamination Activity. Biochem.J. V. 477 1483 2020.
ISSN: ESSN 1470-8728
PubMed: 32270856
DOI: 10.1042/BCJ20190858