Zinc in PDB 1uwy: Crystal Structure of Human Carboxypeptidase M

All present enzymatic activity of Crystal Structure of Human Carboxypeptidase M:
3.4.17.12;

The structure of Crystal Structure of Human Carboxypeptidase M, PDB code: 1uwy was solved by K.Maskos, D.Reverter, W.Bode, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.0 / 3.0
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	85.830, 85.830, 124.540, 90.00, 90.00, 120.00
R / Rfree (%)	20.6 / 28.6

The binding sites of Zinc atom in the Crystal Structure of Human Carboxypeptidase M (pdb code 1uwy). 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 Crystal Structure of Human Carboxypeptidase M, PDB code: 1uwy:

Zinc binding site 1 out of 1 in the Crystal Structure of Human Carboxypeptidase M


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Human Carboxypeptidase M within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1405 b:54.1 occ:1.00 OE2 A:GLU69 2.1 39.1 1.0 ND1 A:HIS173 2.1 46.0 1.0 ND1 A:HIS66 2.2 50.3 1.0 OE1 A:GLU69 2.3 38.4 1.0 CD A:GLU69 2.5 39.0 1.0 CE1 A:HIS66 2.9 50.5 1.0 CG A:HIS173 3.0 45.8 1.0 CE1 A:HIS173 3.0 47.7 1.0 CB A:HIS173 3.4 45.5 1.0 CG A:HIS66 3.4 51.5 1.0 O A:GLY174 3.9 45.6 1.0 CG A:GLU69 4.0 39.9 1.0 CB A:HIS66 4.0 50.0 1.0 NE2 A:HIS173 4.1 46.7 1.0 NH2 A:ARG127 4.1 47.7 1.0 CD2 A:HIS173 4.1 45.4 1.0 NE2 A:HIS66 4.1 50.5 1.0 OE1 A:GLU264 4.1 38.9 1.0 CA A:HIS173 4.3 44.8 1.0 N A:GLY174 4.3 43.7 1.0 CD2 A:HIS66 4.4 51.5 1.0 NZ A:LYS269 4.4 45.6 1.0 OE2 A:GLU264 4.5 39.5 1.0 CD A:GLU264 4.8 40.0 1.0 CB A:GLU69 4.8 42.0 1.0 C A:HIS173 4.8 44.5 1.0 C A:GLY174 4.9 44.6 1.0

D.Reverter, K.Maskos, F.Tan, R.Skidgel, W.Bode. Crystal Structure of Human Carboxypeptidase M, A Membrane-Bound Enzyme That Regulates Peptide Hormone Activity J.Mol.Biol. V. 338 257 2004.
ISSN: ISSN 0022-2836
PubMed: 15066430
DOI: 10.1016/J.JMB.2004.02.058