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Calcium in PDB 5f09: Structure of Inactive Gcpii Mutant in Complex with Beta-Citryl Glutamate

Enzymatic activity of Structure of Inactive Gcpii Mutant in Complex with Beta-Citryl Glutamate

All present enzymatic activity of Structure of Inactive Gcpii Mutant in Complex with Beta-Citryl Glutamate:
3.4.17.21;

Protein crystallography data

The structure of Structure of Inactive Gcpii Mutant in Complex with Beta-Citryl Glutamate, PDB code: 5f09 was solved by J.Tykvart, M.Navratil, P.Pachl, J.Konvalinka, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.85
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 100.901, 130.923, 159.136, 90.00, 90.00, 90.00
R / Rfree (%) 15.5 / 18.1

Other elements in 5f09:

The structure of Structure of Inactive Gcpii Mutant in Complex with Beta-Citryl Glutamate also contains other interesting chemical elements:

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

Calcium Binding Sites:

The binding sites of Calcium atom in the Structure of Inactive Gcpii Mutant in Complex with Beta-Citryl Glutamate (pdb code 5f09). 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 Structure of Inactive Gcpii Mutant in Complex with Beta-Citryl Glutamate, PDB code: 5f09:

Calcium binding site 1 out of 1 in 5f09

Go back to Calcium Binding Sites List in 5f09
Calcium binding site 1 out of 1 in the Structure of Inactive Gcpii Mutant in Complex with Beta-Citryl Glutamate


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of Inactive Gcpii Mutant in Complex with Beta-Citryl Glutamate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca818

b:22.4
occ:1.00
 OE2 A:GLU436 2.3 21.0 1.0
O A:THR269 2.4 21.4 1.0
O A:TYR272 2.4 22.1 1.0
O A:HOH992 2.4 20.3 1.0
OE1 A:GLU433 2.4 21.5 1.0
OE2 A:GLU433 2.5 21.5 1.0
OG1 A:THR269 2.5 20.9 1.0
CD A:GLU433 2.8 21.4 1.0
C A:THR269 3.3 21.8 1.0
CB A:THR269 3.3 21.5 1.0
CD A:GLU436 3.4 21.2 1.0
C A:TYR272 3.5 21.9 1.0
OE1 A:GLU436 3.9 20.7 1.0
CA A:THR269 3.9 22.0 1.0
N A:TYR272 4.0 21.6 1.0
CB A:ASP266 4.2 23.0 1.0
CA A:PRO273 4.2 22.1 1.0
N A:PRO270 4.2 22.4 1.0
N A:ALA274 4.3 22.8 1.0
CG A:GLU433 4.3 21.5 1.0
N A:PRO273 4.3 21.8 1.0
CA A:TYR272 4.4 21.6 1.0
CA A:PRO270 4.4 21.6 1.0
C A:PRO273 4.4 22.1 1.0
O A:ASP266 4.5 22.8 1.0
N A:GLY271 4.5 21.1 1.0
N A:ASP266 4.5 22.5 1.0
O A:ALA264 4.6 23.2 1.0
N A:THR269 4.6 23.2 1.0
CG2 A:THR269 4.7 22.7 1.0
CG A:GLU436 4.7 20.9 1.0
C A:PRO270 4.7 21.8 1.0
OD2 A:ASP266 4.7 23.3 1.0
CA A:ASP266 4.9 22.5 1.0
CB A:ALA274 4.9 24.4 1.0
CB A:GLU436 4.9 22.1 1.0
C A:GLY271 5.0 21.7 1.0

Reference:

M.Navratil, J.Tykvart, J.Schimer, P.Pachl, V.Navratil, T.A.Rokob, K.Hlouchova, L.Rulisek, J.Konvalinka. Comparison of Human Glutamate Carboxypeptidases II and III Reveals Their Divergent Substrate Specificities. Febs J. V. 283 2528 2016.
ISSN: ISSN 1742-464X
PubMed: 27208881
DOI: 10.1111/FEBS.13761
Page generated: Wed Jul 9 05:48:02 2025

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