Zinc in PDB 1lbu: Hydrolase Metallo (Zn) Dd-Peptidase

All present enzymatic activity of Hydrolase Metallo (Zn) Dd-Peptidase:
3.4.17.8;

The structure of Hydrolase Metallo (Zn) Dd-Peptidase, PDB code: 1lbu was solved by P.Charlier, J.-P.Wery, O.Dideberg, J.-M.Frere, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	6.00 / 1.80
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	51.080, 49.700, 38.650, 90.00, 100.60, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Zinc atom in the Hydrolase Metallo (Zn) Dd-Peptidase (pdb code 1lbu). 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 Hydrolase Metallo (Zn) Dd-Peptidase, PDB code: 1lbu:

Zinc binding site 1 out of 1 in the Hydrolase Metallo (Zn) Dd-Peptidase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Hydrolase Metallo (Zn) Dd-Peptidase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn214 b:12.0 occ:1.00 OD1 A:ASP161 2.0 9.8 1.0 O A:HOH234 2.1 16.0 1.0 ND1 A:HIS197 2.1 10.8 1.0 NE2 A:HIS154 2.2 10.7 1.0 CG A:ASP161 2.8 13.9 1.0 OD2 A:ASP161 3.1 16.8 1.0 CE1 A:HIS154 3.1 16.8 1.0 CE1 A:HIS197 3.1 10.3 1.0 CD2 A:HIS154 3.2 13.6 1.0 CG A:HIS197 3.2 11.8 1.0 CB A:HIS197 3.6 10.2 1.0 NE2 A:HIS195 4.2 27.5 1.0 ND1 A:HIS154 4.2 9.6 1.0 CB A:ASP161 4.2 14.5 1.0 CA A:HIS197 4.3 9.3 1.0 NE2 A:HIS197 4.3 6.7 1.0 CG A:HIS154 4.3 9.0 1.0 CD2 A:HIS197 4.3 7.8 1.0 NH1 A:ARG138 4.3 28.9 1.0 O A:HOH271 4.5 21.1 0.6 CD2 A:HIS195 4.6 28.7 1.0 CA A:ASP161 4.6 12.1 1.0 O A:HOH312 4.7 36.6 0.5 O A:ALA160 4.7 12.3 1.0 NE2 A:HIS192 4.7 21.3 1.0 O A:HOH307 4.8 13.3 0.4 N A:ASP161 4.8 11.5 1.0 C A:ALA160 4.9 9.0 1.0 O A:HOH269 4.9 27.4 1.0 O A:HOH306 4.9 45.5 0.9 CB A:ALA159 5.0 14.7 1.0

P.Charlier, J.-P.Wery, O.Dideberg, J.-M.Frere. Streptomyces Albus G D-Ala-A-Ala Carboxypeptidase Handbook of Metalloproteins V. 3 164 2004.