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Calcium in PDB 3rbu: N-Terminally Avitev-Tagged Human Glutamate Carboxypeptidase II in Complex with 2-Pmpa

Enzymatic activity of N-Terminally Avitev-Tagged Human Glutamate Carboxypeptidase II in Complex with 2-Pmpa

All present enzymatic activity of N-Terminally Avitev-Tagged Human Glutamate Carboxypeptidase II in Complex with 2-Pmpa:
3.4.17.21;

Protein crystallography data

The structure of N-Terminally Avitev-Tagged Human Glutamate Carboxypeptidase II in Complex with 2-Pmpa, PDB code: 3rbu was solved by J.Tykvart, P.Sacha, C.Barinka, J.Starkova, T.Knedlik, J.Lubkowski, J.Konvalinka, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.46 / 1.60
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 101.247, 130.559, 158.897, 90.00, 90.00, 90.00
R / Rfree (%) 15.7 / 18.2

Other elements in 3rbu:

The structure of N-Terminally Avitev-Tagged Human Glutamate Carboxypeptidase II in Complex with 2-Pmpa also contains other interesting chemical elements:

Zinc (Zn) 2 atoms
Chlorine (Cl) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the N-Terminally Avitev-Tagged Human Glutamate Carboxypeptidase II in Complex with 2-Pmpa (pdb code 3rbu). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the N-Terminally Avitev-Tagged Human Glutamate Carboxypeptidase II in Complex with 2-Pmpa, PDB code: 3rbu:

Calcium binding site 1 out of 1 in 3rbu

Go back to Calcium Binding Sites List in 3rbu
Calcium binding site 1 out of 1 in the N-Terminally Avitev-Tagged Human Glutamate Carboxypeptidase II in Complex with 2-Pmpa


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of N-Terminally Avitev-Tagged Human Glutamate Carboxypeptidase II in Complex with 2-Pmpa within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca1753

b:16.4
occ:1.00
 OE2 A:GLU436 2.3 17.7 1.0
O A:TYR272 2.3 16.7 1.0
O A:THR269 2.4 16.5 1.0
OE1 A:GLU433 2.5 17.1 1.0
O A:HOH2005 2.5 17.2 1.0
OE2 A:GLU433 2.5 16.9 1.0
OG1 A:THR269 2.5 16.2 1.0
CD A:GLU433 2.8 16.2 1.0
C A:THR269 3.3 16.4 1.0
CB A:THR269 3.3 16.8 1.0
C A:TYR272 3.4 16.2 1.0
CD A:GLU436 3.4 18.0 1.0
CA A:THR269 3.9 17.3 1.0
OE1 A:GLU436 3.9 17.3 1.0
N A:TYR272 4.0 17.2 1.0
CA A:PRO273 4.2 17.1 1.0
CB A:ASP266 4.2 18.7 1.0
N A:PRO270 4.2 17.3 1.0
N A:ALA274 4.3 16.8 1.0
N A:PRO273 4.3 16.9 1.0
CG A:GLU433 4.3 17.1 1.0
CA A:TYR272 4.3 17.4 1.0
C A:PRO273 4.4 17.9 1.0
CA A:PRO270 4.4 17.3 1.0
N A:ASP266 4.5 16.2 1.0
N A:GLY271 4.5 17.4 1.0
O A:ASP266 4.6 18.6 1.0
O A:ALA264 4.6 19.5 1.0
N A:THR269 4.6 17.8 1.0
CG A:GLU436 4.7 15.9 1.0
CG2 A:THR269 4.7 17.8 1.0
C A:PRO270 4.7 17.2 1.0
OD2 A:ASP266 4.7 19.2 1.0
CB A:ALA274 4.9 19.1 1.0
CA A:ASP266 4.9 17.7 1.0
CB A:GLU436 4.9 16.1 1.0
C A:GLY271 5.0 19.3 1.0

Reference:

J.Tykvart, P.Sacha, C.Barinka, T.Knedlik, J.Starkova, J.Lubkowski, J.Konvalinka. Efficient and Versatile One-Step Affinity Purification of in Vivo Biotinylated Proteins: Expression, Characterization and Structure Analysis of Recombinant Human Glutamate Carboxypeptidase II. Protein Expr.Purif. V. 82 106 2012.
ISSN: ISSN 1046-5928
PubMed: 22178733
DOI: 10.1016/J.PEP.2011.11.016
Page generated: Tue Jul 8 16:17:53 2025

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