Zinc in PDB 1rjq: The Crystal Structure of the D-Aminoacylase Mutant D366A

All present enzymatic activity of The Crystal Structure of the D-Aminoacylase Mutant D366A:
3.5.1.81;

The structure of The Crystal Structure of the D-Aminoacylase Mutant D366A, PDB code: 1rjq was solved by W.L.Lai, L.Y.Chou, C.Y.Ting, Y.C.Tsai, S.H.Liaw, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	32.40 / 1.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	60.019, 76.927, 135.586, 90.00, 90.00, 90.00
R / Rfree (%)	18 / 20.2

The binding sites of Zinc atom in the The Crystal Structure of the D-Aminoacylase Mutant D366A (pdb code 1rjq). 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 Crystal Structure of the D-Aminoacylase Mutant D366A, PDB code: 1rjq:

Zinc binding site 1 out of 1 in the The Crystal Structure of the D-Aminoacylase Mutant D366A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Crystal Structure of the D-Aminoacylase Mutant D366A within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn601 b:14.6 occ:1.00 O A:ACT901 2.0 14.5 1.0 ND1 A:HIS220 2.0 11.1 1.0 NE2 A:HIS250 2.1 14.0 1.0 SG A:CYS96 2.2 13.1 1.0 C A:ACT901 2.7 14.5 1.0 OXT A:ACT901 2.8 14.2 1.0 CE1 A:HIS220 2.9 12.8 1.0 CG A:HIS220 3.0 12.3 1.0 CE1 A:HIS250 3.1 13.8 1.0 CD2 A:HIS250 3.1 13.3 1.0 CB A:CYS96 3.3 13.5 1.0 CB A:HIS220 3.4 10.8 1.0 OH A:TYR192 4.0 13.3 1.0 NE2 A:HIS220 4.0 12.3 1.0 CD2 A:HIS220 4.1 11.1 1.0 NE2 A:HIS67 4.1 12.3 1.0 CH3 A:ACT901 4.2 15.2 1.0 ND1 A:HIS250 4.2 12.5 1.0 CG A:HIS250 4.3 12.6 1.0 CH3 A:ACT902 4.3 13.9 1.0 CE2 A:TYR192 4.3 13.8 1.0 CE1 A:HIS67 4.4 10.6 1.0 CA A:CYS96 4.5 12.2 1.0 CA A:HIS220 4.5 12.4 1.0 CZ A:TYR192 4.6 14.7 1.0 NE2 A:HIS69 4.8 14.2 1.0 CE1 A:HIS69 5.0 12.7 1.0

W.L.Lai, L.Y.Chou, C.Y.Ting, R.Kirby, Y.C.Tsai, A.H.Wang, S.H.Liaw. The Functional Role of the Binuclear Metal Center in D-Aminoacylase: One-Metal Activation and Second-Metal Attenuation. J.Biol.Chem. V. 279 13962 2004.
ISSN: ISSN 0021-9258
PubMed: 14736882
DOI: 10.1074/JBC.M308849200