Zinc in PDB 2or4: A High Resolution Crystal Structure of Human Glutamate Carboxypeptidase II in Complex with Quisqualic Acid

All present enzymatic activity of A High Resolution Crystal Structure of Human Glutamate Carboxypeptidase II in Complex with Quisqualic Acid:
3.4.17.21;

The structure of A High Resolution Crystal Structure of Human Glutamate Carboxypeptidase II in Complex with Quisqualic Acid, PDB code: 2or4 was solved by C.Barinka, J.Lubkowski, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.62
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	102.007, 130.437, 159.508, 90.00, 90.00, 90.00
R / Rfree (%)	18.4 / 21.9

The structure of A High Resolution Crystal Structure of Human Glutamate Carboxypeptidase II in Complex with Quisqualic Acid also contains other interesting chemical elements:

Chlorine	(Cl)	1 atom
Calcium	(Ca)	1 atom

The binding sites of Zinc atom in the A High Resolution Crystal Structure of Human Glutamate Carboxypeptidase II in Complex with Quisqualic Acid (pdb code 2or4). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the A High Resolution Crystal Structure of Human Glutamate Carboxypeptidase II in Complex with Quisqualic Acid, PDB code: 2or4:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the A High Resolution Crystal Structure of Human Glutamate Carboxypeptidase II in Complex with Quisqualic Acid


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of A High Resolution Crystal Structure of Human Glutamate Carboxypeptidase II in Complex with Quisqualic Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1751 b:20.4 occ:1.00 OD2 A:ASP387 2.0 19.8 1.0 O A:HOH2675 2.0 17.4 1.0 OE2 A:GLU425 2.1 17.1 1.0 NE2 A:HIS553 2.1 16.8 1.0 OE1 A:GLU425 2.4 15.7 1.0 CD A:GLU425 2.5 15.5 1.0 CG A:ASP387 3.0 17.5 1.0 CE1 A:HIS553 3.1 17.5 1.0 CD2 A:HIS553 3.1 17.4 1.0 ZN A:ZN1752 3.3 18.3 1.0 OD1 A:ASP387 3.3 18.1 1.0 O A:HOH2296 3.5 26.8 1.0 O A:HOH1816 4.0 18.6 1.0 CG A:GLU425 4.1 15.1 1.0 OE1 A:GLU424 4.1 16.9 1.0 CE1 A:TYR552 4.1 20.1 1.0 ND1 A:HIS553 4.2 16.3 1.0 CG A:HIS553 4.2 16.3 1.0 OH A:TYR552 4.3 19.0 1.0 CB A:ASP387 4.3 17.6 1.0 CD1 A:TRP381 4.4 17.4 1.0 NE2 A:HIS377 4.4 16.0 1.0 C02 A:QUS1801 4.5 19.0 1.0 NP3 A:QUS1801 4.5 17.8 1.0 CE1 A:HIS377 4.5 13.4 1.0 CZ A:TYR552 4.5 17.3 1.0 C01 A:QUS1801 4.6 21.2 1.0 NE1 A:TRP381 4.7 16.4 1.0 O17 A:QUS1801 4.8 17.8 1.0 OD2 A:ASP453 4.9 17.6 1.0

Zinc binding site 2 out of 2 in the A High Resolution Crystal Structure of Human Glutamate Carboxypeptidase II in Complex with Quisqualic Acid


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of A High Resolution Crystal Structure of Human Glutamate Carboxypeptidase II in Complex with Quisqualic Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1752 b:18.3 occ:1.00 OD2 A:ASP453 2.0 17.6 1.0 OD1 A:ASP387 2.0 18.1 1.0 O A:HOH2675 2.0 17.4 1.0 NE2 A:HIS377 2.0 16.0 1.0 CG A:ASP453 2.7 18.2 1.0 OD1 A:ASP453 2.8 18.8 1.0 CG A:ASP387 2.9 17.5 1.0 CE1 A:HIS377 3.0 13.4 1.0 CD2 A:HIS377 3.1 15.3 1.0 ZN A:ZN1751 3.3 20.4 1.0 OD2 A:ASP387 3.3 19.8 1.0 OE1 A:GLU424 3.6 16.9 1.0 OE2 A:GLU425 3.7 17.1 1.0 O A:HOH2296 4.1 26.8 1.0 ND1 A:HIS377 4.1 15.1 1.0 CD A:GLU424 4.1 17.6 1.0 CB A:ASP453 4.2 18.6 1.0 O A:HOH2295 4.2 37.5 1.0 CG A:HIS377 4.2 14.2 1.0 CB A:ASP387 4.2 17.6 1.0 ND2 A:ASN519 4.3 17.6 1.0 CB A:PRO388 4.4 16.1 1.0 OE2 A:GLU424 4.4 16.7 1.0 CD A:GLU425 4.4 15.5 1.0 CA A:ASP387 4.6 17.6 1.0 CA A:PRO388 4.6 15.3 1.0 C A:ASP387 4.6 16.4 1.0 N A:PRO388 4.7 16.5 1.0 OE1 A:GLU425 4.7 15.7 1.0 NP3 A:QUS1801 4.8 17.8 1.0 OG A:SER454 4.8 18.6 1.0 O A:HOH2492 4.9 44.3 1.0 CG A:GLU424 4.9 14.4 1.0

C.Barinka, M.Rovenska, P.Mlcochova, K.Hlouchova, A.Plechanovova, P.Majer, T.Tsukamoto, B.S.Slusher, J.Konvalinka, J.Lubkowski. Structural Insight Into the Pharmacophore Pocket of Human Glutamate Carboxypeptidase II. J.Med.Chem. V. 50 3267 2007.
ISSN: ISSN 0022-2623
PubMed: 17567119
DOI: 10.1021/JM070133W