Zinc in PDB 1rk6: The Enzyme in Complex with 50MM CDCL2

All present enzymatic activity of The Enzyme in Complex with 50MM CDCL2:
3.5.1.81;

The structure of The Enzyme in Complex with 50MM CDCL2, PDB code: 1rk6 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)	39.00 / 1.43
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	59.929, 76.936, 135.569, 90.00, 90.00, 90.00
R / Rfree (%)	18.8 / 20.2

The structure of The Enzyme in Complex with 50MM CDCL2 also contains other interesting chemical elements:

Cadmium

(Cd)

1 atom

The binding sites of Zinc atom in the The Enzyme in Complex with 50MM CDCL2 (pdb code 1rk6). 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 Enzyme in Complex with 50MM CDCL2, PDB code: 1rk6:

Zinc binding site 1 out of 1 in the The Enzyme in Complex with 50MM CDCL2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Enzyme in Complex with 50MM CDCL2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn601 b:7.8 occ:1.00 NE2 A:HIS250 2.0 6.3 1.0 O A:ACT901 2.1 8.1 1.0 ND1 A:HIS220 2.1 6.5 1.0 SG A:CYS96 2.2 7.7 1.0 OXT A:ACT901 2.6 8.9 1.0 C A:ACT901 2.6 9.9 1.0 CE1 A:HIS250 3.0 6.7 1.0 CE1 A:HIS220 3.0 6.4 1.0 CD2 A:HIS250 3.0 6.4 1.0 CG A:HIS220 3.1 6.5 1.0 CB A:CYS96 3.3 7.2 1.0 CB A:HIS220 3.4 6.0 1.0 CD A:CD602 3.6 35.6 1.0 NE2 A:HIS220 4.1 7.0 1.0 ND1 A:HIS250 4.1 6.4 1.0 CH3 A:ACT901 4.1 9.3 1.0 CD2 A:HIS220 4.1 7.4 1.0 OH A:TYR192 4.2 9.4 1.0 CH3 A:ACT902 4.2 10.0 1.0 CG A:HIS250 4.2 5.6 1.0 NE2 A:HIS67 4.3 6.4 1.0 CE2 A:TYR192 4.3 8.5 1.0 CE1 A:HIS67 4.3 6.6 1.0 CA A:HIS220 4.5 7.1 1.0 CA A:CYS96 4.5 7.2 1.0 CZ A:TYR192 4.7 8.8 1.0 NE2 A:HIS69 4.8 6.9 1.0 OD2 A:ASP366 4.9 10.7 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