Zinc in PDB 2cij: Membrane-Bound Glutamate Carboxypeptidase II (Gcpii) with Bound Methionine

All present enzymatic activity of Membrane-Bound Glutamate Carboxypeptidase II (Gcpii) with Bound Methionine:
3.4.17.21;

The structure of Membrane-Bound Glutamate Carboxypeptidase II (Gcpii) with Bound Methionine, PDB code: 2cij was solved by C.Barinka, A.Plechanovova, L.Rulisek, P.Mlcochova, P.Majer, B.S.Slusher, R.Hilgenfeld, J.R.Mesters, J.Konvalinka, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.40
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	102.692, 130.777, 160.303, 90.00, 90.00, 90.00
R / Rfree (%)	17.2 / 21.9

The structure of Membrane-Bound Glutamate Carboxypeptidase II (Gcpii) with Bound Methionine also contains other interesting chemical elements:

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

The binding sites of Zinc atom in the Membrane-Bound Glutamate Carboxypeptidase II (Gcpii) with Bound Methionine (pdb code 2cij). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Membrane-Bound Glutamate Carboxypeptidase II (Gcpii) with Bound Methionine, PDB code: 2cij:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Membrane-Bound Glutamate Carboxypeptidase II (Gcpii) with Bound Methionine


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Membrane-Bound Glutamate Carboxypeptidase II (Gcpii) with Bound Methionine within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1751 b:18.9 occ:1.00 OD2 A:ASP387 2.0 17.1 1.0 OE2 A:GLU425 2.0 11.1 1.0 NE2 A:HIS553 2.1 22.1 1.0 O A:HOH2218 2.3 17.9 1.0 OE1 A:GLU425 2.4 11.9 1.0 CD A:GLU425 2.5 10.5 1.0 CG A:ASP387 3.0 21.3 1.0 CE1 A:HIS553 3.1 22.5 1.0 CD2 A:HIS553 3.1 17.8 1.0 O A:HOH2223 3.1 52.5 1.0 ZN A:ZN1752 3.3 18.4 1.0 OD1 A:ASP387 3.4 25.9 1.0 N A:MET2000 4.0 19.8 1.0 OE1 A:GLU424 4.0 24.0 1.0 CG A:GLU425 4.0 11.9 1.0 O A:HOH2090 4.1 12.6 1.0 CE1 A:TYR552 4.2 19.2 1.0 CA A:MET2000 4.2 21.8 1.0 ND1 A:HIS553 4.2 21.8 1.0 CG A:HIS553 4.2 22.8 1.0 CB A:ASP387 4.3 18.9 1.0 OH A:TYR552 4.4 20.2 1.0 NE2 A:HIS377 4.4 16.1 1.0 CE1 A:HIS377 4.4 15.1 1.0 CD1 A:TRP381 4.5 18.7 1.0 C A:MET2000 4.6 21.3 1.0 CZ A:TYR552 4.6 19.4 1.0 NE1 A:TRP381 4.7 20.2 1.0 OXT A:MET2000 4.8 20.6 1.0 OD2 A:ASP453 4.9 21.3 1.0 CB A:GLU425 5.0 14.2 1.0

Zinc binding site 2 out of 2 in the Membrane-Bound Glutamate Carboxypeptidase II (Gcpii) with Bound Methionine


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Membrane-Bound Glutamate Carboxypeptidase II (Gcpii) with Bound Methionine within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1752 b:18.4 occ:1.00 O A:HOH2218 1.8 17.9 1.0 OD2 A:ASP453 1.9 21.3 1.0 NE2 A:HIS377 2.0 16.1 1.0 OD1 A:ASP387 2.1 25.9 1.0 CG A:ASP453 2.7 21.5 1.0 OD1 A:ASP453 2.8 23.1 1.0 CE1 A:HIS377 2.9 15.1 1.0 CG A:ASP387 2.9 21.3 1.0 CD2 A:HIS377 3.1 19.8 1.0 OD2 A:ASP387 3.1 17.1 1.0 ZN A:ZN1751 3.3 18.9 1.0 OE1 A:GLU424 3.6 24.0 1.0 O A:HOH2223 3.6 52.5 1.0 OE2 A:GLU425 3.7 11.1 1.0 ND1 A:HIS377 4.0 15.0 1.0 CD A:GLU424 4.1 17.2 1.0 CB A:ASP453 4.1 19.6 1.0 CG A:HIS377 4.2 16.9 1.0 ND2 A:ASN519 4.2 18.9 1.0 CB A:ASP387 4.3 18.9 1.0 CB A:PRO388 4.3 17.9 1.0 OE2 A:GLU424 4.4 19.0 1.0 CD A:GLU425 4.5 10.5 1.0 CA A:PRO388 4.6 18.0 1.0 N A:PRO388 4.6 18.5 1.0 N A:MET2000 4.6 19.8 1.0 CA A:ASP387 4.6 19.8 1.0 C A:ASP387 4.6 18.7 1.0 OE1 A:GLU425 4.8 11.9 1.0 OG A:SER454 4.8 20.8 1.0

J.R.Mesters, R.Hilgenfeld. Glutamate Carboxypeptidase II Handbook of Metalloproteins V. 4 681 2011.