Zinc in PDB 4jz0: X-Ray Structure of Human Glutamate Carboxypeptidase II (Gcpii) in Complex with CTT1055

All present enzymatic activity of X-Ray Structure of Human Glutamate Carboxypeptidase II (Gcpii) in Complex with CTT1055:
3.4.17.21;

The structure of X-Ray Structure of Human Glutamate Carboxypeptidase II (Gcpii) in Complex with CTT1055, PDB code: 4jz0 was solved by C.Barinka, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.59 / 1.83
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	101.819, 130.399, 159.987, 90.00, 90.00, 90.00
R / Rfree (%)	15.2 / 17.1

The structure of X-Ray Structure of Human Glutamate Carboxypeptidase II (Gcpii) in Complex with CTT1055 also contains other interesting chemical elements:

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

The binding sites of Zinc atom in the X-Ray Structure of Human Glutamate Carboxypeptidase II (Gcpii) in Complex with CTT1055 (pdb code 4jz0). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the X-Ray Structure of Human Glutamate Carboxypeptidase II (Gcpii) in Complex with CTT1055, PDB code: 4jz0:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the X-Ray Structure of Human Glutamate Carboxypeptidase II (Gcpii) in Complex with CTT1055


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of X-Ray Structure of Human Glutamate Carboxypeptidase II (Gcpii) in Complex with CTT1055 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn801 b:27.6 occ:1.00 OE2 A:GLU425 1.9 25.1 1.0 OD2 A:ASP387 1.9 29.1 1.0 OAL A:T01818 1.9 27.3 1.0 NE2 A:HIS553 2.1 29.0 1.0 OE1 A:GLU425 2.5 26.3 1.0 CD A:GLU425 2.6 25.1 1.0 OAG A:T01818 2.9 22.9 1.0 PBL A:T01818 2.9 25.4 1.0 CG A:ASP387 3.0 30.8 1.0 CE1 A:HIS553 3.1 30.4 1.0 CD2 A:HIS553 3.1 29.0 1.0 OD1 A:ASP387 3.5 26.1 1.0 ZN A:ZN802 3.6 27.6 1.0 CE1 A:TYR552 3.7 27.9 1.0 O A:HOH2015 3.8 19.7 1.0 OH A:TYR552 3.9 26.5 1.0 NAY A:T01818 4.0 27.6 1.0 CBJ A:T01818 4.0 27.2 1.0 OAZ A:T01818 4.1 25.6 1.0 CG A:GLU425 4.1 26.1 1.0 CZ A:TYR552 4.1 28.3 1.0 ND1 A:HIS553 4.2 28.7 1.0 CG A:HIS553 4.2 29.6 1.0 CB A:ASP387 4.3 27.1 1.0 CBC A:T01818 4.4 28.5 1.0 CD1 A:TRP381 4.5 28.2 1.0 OE1 A:GLU424 4.5 23.8 1.0 OAJ A:T01818 4.6 29.0 1.0 NE1 A:TRP381 4.7 29.7 1.0 CD1 A:TYR552 4.7 28.9 1.0 NE2 A:HIS377 4.7 25.4 1.0 CE1 A:HIS377 4.8 28.8 1.0 O A:HOH2054 5.0 22.0 1.0

Zinc binding site 2 out of 2 in the X-Ray Structure of Human Glutamate Carboxypeptidase II (Gcpii) in Complex with CTT1055


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of X-Ray Structure of Human Glutamate Carboxypeptidase II (Gcpii) in Complex with CTT1055 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn802 b:27.6 occ:1.00 OAG A:T01818 1.7 22.9 1.0 NE2 A:HIS377 1.9 25.4 1.0 OD2 A:ASP453 2.0 27.6 1.0 OD1 A:ASP387 2.1 26.1 1.0 CG A:ASP453 2.8 26.5 1.0 OD1 A:ASP453 2.9 29.1 1.0 CE1 A:HIS377 2.9 28.8 1.0 CD2 A:HIS377 2.9 22.7 1.0 CG A:ASP387 3.0 30.8 1.0 PBL A:T01818 3.3 25.4 1.0 OD2 A:ASP387 3.3 29.1 1.0 OE2 A:GLU425 3.5 25.1 1.0 ZN A:ZN801 3.6 27.6 1.0 OE1 A:GLU424 3.8 23.8 1.0 OAZ A:T01818 3.9 25.6 1.0 OAL A:T01818 4.0 27.3 1.0 ND1 A:HIS377 4.0 25.2 1.0 CG A:HIS377 4.1 25.4 1.0 ND2 A:ASN519 4.1 25.6 1.0 CD A:GLU424 4.2 26.3 1.0 CB A:ASP453 4.2 26.6 1.0 CB A:ASP387 4.3 27.1 1.0 O A:HOH2399 4.3 39.6 1.0 OE2 A:GLU424 4.3 25.3 1.0 CB A:PRO388 4.3 26.1 1.0 CD A:GLU425 4.4 25.1 1.0 NAY A:T01818 4.5 27.6 1.0 CA A:PRO388 4.6 27.2 1.0 CA A:ASP387 4.6 27.9 1.0 C A:ASP387 4.6 27.5 1.0 N A:PRO388 4.7 26.8 1.0 OG A:SER454 4.7 28.6 1.0 OE1 A:GLU425 4.9 26.3 1.0 CG A:ASN519 5.0 24.9 1.0 OD1 A:ASN519 5.0 26.1 1.0

T.Ganguly, S.Dannoon, J.G.Geruntho, M.R.Hopkins, S.Murphy, H.Cahaya, J.E.Blecha, S.Jivan, C.Barinka, E.F.Jones, H.F.Vanbrocklin, C.E.Berkman. A High Affinity 18F-Labeled Phosphoramidate Peptidomimetic Inhibitor As A Psma-Targeted Pet Imaging Agent For Prostate Cancer To Be Published.