Zinc in PDB 1qmu: Duck Carboxypeptidase D Domain II

The structure of Duck Carboxypeptidase D Domain II, PDB code: 1qmu was solved by F.X.Gomis-Rueth, M.Coll, F.X.Aviles, J.Vendrell, L.D.Fricker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.70
Space group	P 21 3
Cell size a, b, c (Å), α, β, γ (°)	135.540, 135.540, 135.540, 90.00, 90.00, 90.00
R / Rfree (%)	19.8 / 23.6

The binding sites of Zinc atom in the Duck Carboxypeptidase D Domain II (pdb code 1qmu). 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 Duck Carboxypeptidase D Domain II, PDB code: 1qmu:

Zinc binding site 1 out of 1 in the Duck Carboxypeptidase D Domain II


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Duck Carboxypeptidase D Domain II within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn999 b:51.8 occ:1.00 ND1 A:HIS74 2.0 45.4 1.0 ND1 A:HIS181 2.1 47.5 1.0 OE1 A:GLU77 2.2 44.1 1.0 OE2 A:GLU77 2.3 47.2 1.0 CE1 A:HIS74 2.6 46.0 1.0 CD A:GLU77 2.6 45.2 1.0 O A:HOH2121 2.7 36.9 1.0 CE1 A:HIS181 3.0 47.2 1.0 CG A:HIS181 3.1 47.3 1.0 CG A:HIS74 3.3 47.0 1.0 CB A:HIS181 3.5 47.1 1.0 O3 A:SO4998 3.6 55.1 0.7 NH1 A:ARG135 3.9 54.3 1.0 NE2 A:HIS74 3.9 44.4 1.0 OE2 A:GLU272 3.9 48.9 1.0 O2 A:SO4998 3.9 53.9 0.7 CB A:HIS74 4.0 49.3 1.0 O A:GLY182 4.1 48.1 1.0 CG A:GLU77 4.1 45.1 1.0 NE2 A:HIS181 4.1 45.7 1.0 CD2 A:HIS74 4.2 44.3 1.0 CD2 A:HIS181 4.2 44.1 1.0 S A:SO4998 4.2 55.5 0.7 N A:GLY182 4.4 47.2 1.0 CA A:HIS181 4.5 47.2 1.0 O1 A:SO4998 4.5 52.1 0.7 CD A:GLU272 4.8 47.8 1.0 CZ A:ARG135 4.8 54.4 1.0 OE1 A:GLU272 4.9 47.3 1.0 CB A:GLU77 4.9 46.0 1.0

F.X.Gomis-Rueth, V.Companys, Y.Qian, L.D.Fricker, J.Vendrell, F.X.Aviles, M.Coll. Crystal Structure of Avian Carboxypeptidase D Domain II : A Prototype For the Regulatory Metallocarboxypeptidase Subfamily Embo J. V. 18 5817 1999.
ISSN: ISSN 0261-4189
PubMed: 10545093
DOI: 10.1093/EMBOJ/18.21.5817