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Zinc in PDB 2oot: A High Resolution Structure of Ligand-Free Human Glutamate Carboxypeptidase II

Enzymatic activity of A High Resolution Structure of Ligand-Free Human Glutamate Carboxypeptidase II

All present enzymatic activity of A High Resolution Structure of Ligand-Free Human Glutamate Carboxypeptidase II:
3.4.17.21;

Protein crystallography data

The structure of A High Resolution Structure of Ligand-Free Human Glutamate Carboxypeptidase II, PDB code: 2oot 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 / 1.64
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 101.759, 130.128, 158.874, 90.00, 90.00, 90.00
R / Rfree (%) 20.6 / 22.8

Other elements in 2oot:

The structure of A High Resolution Structure of Ligand-Free Human Glutamate Carboxypeptidase II also contains other interesting chemical elements:

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

Zinc Binding Sites:

The binding sites of Zinc atom in the A High Resolution Structure of Ligand-Free Human Glutamate Carboxypeptidase II (pdb code 2oot). 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 Structure of Ligand-Free Human Glutamate Carboxypeptidase II, PDB code: 2oot:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 2oot

Go back to Zinc Binding Sites List in 2oot
Zinc binding site 1 out of 2 in the A High Resolution Structure of Ligand-Free Human Glutamate Carboxypeptidase II


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 Structure of Ligand-Free Human Glutamate Carboxypeptidase II within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1751

b:21.0
occ:1.00
NE2 A:HIS553 2.0 20.2 1.0
OD2 A:ASP387 2.0 20.1 1.0
O A:HOH2265 2.0 22.1 1.0
OE2 A:GLU425 2.1 16.8 1.0
OE1 A:GLU425 2.5 17.3 1.0
O A:HOH2325 2.5 40.2 1.0
CD A:GLU425 2.6 13.9 1.0
CG A:ASP387 2.9 18.0 1.0
CE1 A:HIS553 3.0 18.7 1.0
CD2 A:HIS553 3.1 20.6 1.0
OD1 A:ASP387 3.3 20.2 1.0
ZN A:ZN1752 3.4 18.9 1.0
O A:HOH2271 3.8 38.3 1.0
O A:HOH1782 4.0 19.8 1.0
ND1 A:HIS553 4.1 18.4 1.0
CG A:GLU425 4.1 17.0 1.0
CE1 A:TYR552 4.1 21.8 1.0
CG A:HIS553 4.2 19.2 1.0
OE1 A:GLU424 4.2 21.5 1.0
OH A:TYR552 4.2 25.9 1.0
CB A:ASP387 4.3 17.6 1.0
O A:HOH2270 4.3 30.9 1.0
NE2 A:HIS377 4.5 15.5 1.0
CZ A:TYR552 4.5 22.0 1.0
CD1 A:TRP381 4.6 19.1 1.0
CE1 A:HIS377 4.6 13.9 1.0
O A:HOH2268 4.7 27.4 1.0
NE1 A:TRP381 4.7 21.1 1.0
OD2 A:ASP453 5.0 18.9 1.0

Zinc binding site 2 out of 2 in 2oot

Go back to Zinc Binding Sites List in 2oot
Zinc binding site 2 out of 2 in the A High Resolution Structure of Ligand-Free Human Glutamate Carboxypeptidase II


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 Structure of Ligand-Free Human Glutamate Carboxypeptidase II within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1752

b:18.9
occ:1.00
OD2 A:ASP453 1.9 18.9 1.0
OD1 A:ASP387 2.0 20.2 1.0
O A:HOH2265 2.0 22.1 1.0
NE2 A:HIS377 2.1 15.5 1.0
CG A:ASP453 2.6 20.4 1.0
OD1 A:ASP453 2.7 22.3 1.0
CG A:ASP387 2.9 18.0 1.0
CE1 A:HIS377 3.0 13.9 1.0
CD2 A:HIS377 3.1 14.7 1.0
OD2 A:ASP387 3.3 20.1 1.0
ZN A:ZN1751 3.4 21.0 1.0
O A:HOH2271 3.7 38.3 1.0
OE1 A:GLU424 3.7 21.5 1.0
OE2 A:GLU425 3.8 16.8 1.0
O A:HOH2277 3.9 46.7 1.0
CB A:ASP453 4.1 19.4 1.0
ND1 A:HIS377 4.2 15.9 1.0
CB A:ASP387 4.2 17.6 1.0
CG A:HIS377 4.2 12.5 1.0
CD A:GLU424 4.2 21.3 1.0
ND2 A:ASN519 4.3 20.9 1.0
CB A:PRO388 4.3 15.5 1.0
O A:HOH2325 4.3 40.2 1.0
OE2 A:GLU424 4.4 21.5 1.0
O A:HOH2270 4.5 30.9 1.0
CD A:GLU425 4.5 13.9 1.0
CA A:PRO388 4.6 15.3 1.0
CA A:ASP387 4.6 17.4 1.0
N A:PRO388 4.7 16.7 1.0
C A:ASP387 4.7 17.9 1.0
OG A:SER454 4.8 13.2 0.5
OE1 A:GLU425 4.8 17.3 1.0
O A:HOH2278 4.9 44.2 1.0

Reference:

C.Barinka, J.Starkova, J.Konvalinka, J.Lubkowski. A High-Resolution Structure of Ligand-Free Human Glutamate Carboxypeptidase II. Acta Crystallogr.,Sect.F V. 63 150 2007.
ISSN: ESSN 1744-3091
PubMed: 17329803
DOI: 10.1107/S174430910700379X
Page generated: Thu Oct 17 02:42:33 2024

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