Zinc in PDB 6h7z: X-Ray Structure of Human Glutamate Carboxypeptidase II (Gcpii) in Complex with A Inhibitor Rna 2-65-1

All present enzymatic activity of X-Ray Structure of Human Glutamate Carboxypeptidase II (Gcpii) in Complex with A Inhibitor Rna 2-65-1:
3.4.17.21;

The structure of X-Ray Structure of Human Glutamate Carboxypeptidase II (Gcpii) in Complex with A Inhibitor Rna 2-65-1, PDB code: 6h7z was solved by L.Motlova, Z.Novakova, C.Barinka, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.00
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	101.222, 130.389, 158.469, 90.00, 90.00, 90.00
R / Rfree (%)	17 / 20.6

The structure of X-Ray Structure of Human Glutamate Carboxypeptidase II (Gcpii) in Complex with A Inhibitor Rna 2-65-1 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 A Inhibitor Rna 2-65-1 (pdb code 6h7z). 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 A Inhibitor Rna 2-65-1, PDB code: 6h7z:
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 A Inhibitor Rna 2-65-1


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 A Inhibitor Rna 2-65-1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn801 b:15.3 occ:1.00 O A:HOH1152 1.8 9.5 1.0 NE2 A:HIS553 2.0 13.4 1.0 OD2 A:ASP387 2.0 13.5 1.0 OE2 A:GLU425 2.0 12.2 1.0 OE1 A:GLU425 2.4 10.8 1.0 CD A:GLU425 2.6 10.9 1.0 OAH A:FVW832 2.7 15.5 1.0 CE1 A:HIS553 2.9 13.1 1.0 CG A:ASP387 3.0 13.1 1.0 CD2 A:HIS553 3.1 13.4 1.0 ZN A:ZN802 3.3 15.5 1.0 OD1 A:ASP387 3.3 13.4 1.0 CAE A:FVW832 3.5 15.9 1.0 NAF A:FVW832 4.0 15.8 1.0 CAG A:FVW832 4.0 15.8 1.0 CG A:GLU425 4.0 10.8 1.0 ND1 A:HIS553 4.1 13.1 1.0 OE1 A:GLU424 4.1 10.6 1.0 O A:HOH1058 4.1 9.5 1.0 CE1 A:TYR552 4.1 13.8 1.0 CG A:HIS553 4.2 13.3 1.0 CB A:ASP387 4.2 12.9 1.0 N A:FVW832 4.4 16.3 1.0 OH A:TYR552 4.4 13.0 1.0 NE2 A:HIS377 4.5 12.3 1.0 CA A:FVW832 4.6 18.4 1.0 CAJ A:FVW832 4.6 15.8 1.0 CZ A:TYR552 4.6 13.4 1.0 CE1 A:HIS377 4.7 12.1 1.0 CD1 A:TRP381 4.7 13.7 1.0 NE1 A:TRP381 4.9 13.9 1.0 OD2 A:ASP453 4.9 15.8 1.0 OBB A:FVW832 4.9 17.2 1.0 CD A:GLU424 5.0 10.8 1.0

Zinc binding site 2 out of 2 in the X-Ray Structure of Human Glutamate Carboxypeptidase II (Gcpii) in Complex with A Inhibitor Rna 2-65-1


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 A Inhibitor Rna 2-65-1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn802 b:15.5 occ:1.00 O A:HOH1152 1.9 9.5 1.0 OD2 A:ASP453 2.0 15.8 1.0 OD1 A:ASP387 2.0 13.4 1.0 NE2 A:HIS377 2.0 12.3 1.0 CG A:ASP453 2.7 15.2 1.0 OD1 A:ASP453 2.9 15.8 1.0 CG A:ASP387 2.9 13.1 1.0 CE1 A:HIS377 2.9 12.1 1.0 CD2 A:HIS377 3.0 12.6 1.0 OD2 A:ASP387 3.1 13.5 1.0 ZN A:ZN801 3.3 15.3 1.0 OE2 A:GLU425 3.6 12.2 1.0 OE1 A:GLU424 3.7 10.6 1.0 CD A:GLU424 4.0 10.8 1.0 ND1 A:HIS377 4.1 11.6 1.0 CG A:HIS377 4.2 11.7 1.0 CB A:ASP453 4.2 15.0 1.0 CB A:ASP387 4.2 12.9 1.0 OE2 A:GLU424 4.2 11.4 1.0 ND2 A:ASN519 4.2 11.7 1.0 CD A:GLU425 4.3 10.9 1.0 CB A:PRO388 4.4 11.9 1.0 CA A:PRO388 4.5 12.0 1.0 CAE A:FVW832 4.5 15.9 1.0 OAH A:FVW832 4.6 15.5 1.0 CA A:ASP387 4.6 12.4 1.0 C A:ASP387 4.6 12.2 1.0 N A:PRO388 4.6 11.8 1.0 OE1 A:GLU425 4.7 10.8 1.0 N A:FVW832 4.7 16.3 1.0 CA A:FVW832 4.7 18.4 1.0 O A:HOH1041 4.8 23.2 1.0 OG A:SER454 4.8 15.5 1.0 CG A:GLU424 4.9 10.3 1.0 NAF A:FVW832 5.0 15.8 1.0

R.Nakajima, Z.Novakova, W.Tueckmantel, L.Motlova, C.Barinka, A.P.Kozikowski. 2-Aminoadipic Acid-C(O)-Glutamate Based Prostate-Specific Membrane Antigen Ligands For Potential Use As Theranostics. Acs Med Chem Lett V. 9 1099 2018.
ISSN: ISSN 1948-5875
PubMed: 30429952
DOI: 10.1021/ACSMEDCHEMLETT.8B00318