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Calcium in PDB 3fec: Crystal Structure of Human Glutamate Carboxypeptidase III (Gcpiii/Naaladase II), Pseudo-Unliganded

Enzymatic activity of Crystal Structure of Human Glutamate Carboxypeptidase III (Gcpiii/Naaladase II), Pseudo-Unliganded

All present enzymatic activity of Crystal Structure of Human Glutamate Carboxypeptidase III (Gcpiii/Naaladase II), Pseudo-Unliganded:
3.4.17.21;

Protein crystallography data

The structure of Crystal Structure of Human Glutamate Carboxypeptidase III (Gcpiii/Naaladase II), Pseudo-Unliganded, PDB code: 3fec was solved by C.Barinka, J.Lubkowski, K.Hlouchova, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.49
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 122.767, 104.322, 78.008, 90.00, 107.69, 90.00
R / Rfree (%) 15.9 / 18.3

Other elements in 3fec:

The structure of Crystal Structure of Human Glutamate Carboxypeptidase III (Gcpiii/Naaladase II), Pseudo-Unliganded also contains other interesting chemical elements:

Chlorine (Cl) 1 atom
Zinc (Zn) 4 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Human Glutamate Carboxypeptidase III (Gcpiii/Naaladase II), Pseudo-Unliganded (pdb code 3fec). 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 Crystal Structure of Human Glutamate Carboxypeptidase III (Gcpiii/Naaladase II), Pseudo-Unliganded, PDB code: 3fec:

Calcium binding site 1 out of 1 in 3fec

Go back to Calcium Binding Sites List in 3fec
Calcium binding site 1 out of 1 in the Crystal Structure of Human Glutamate Carboxypeptidase III (Gcpiii/Naaladase II), Pseudo-Unliganded


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Human Glutamate Carboxypeptidase III (Gcpiii/Naaladase II), Pseudo-Unliganded within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca1755

b:16.8
occ:1.00
 OE2 A:GLU426 2.3 17.9 1.0
O A:TYR262 2.4 17.4 1.0
O A:HOH816 2.4 15.3 1.0
OE1 A:GLU423 2.4 17.2 1.0
OE2 A:GLU423 2.4 16.5 1.0
O A:THR259 2.5 17.4 1.0
OG1 A:THR259 2.5 17.5 1.0
CD A:GLU423 2.8 16.7 1.0
C A:THR259 3.3 17.9 1.0
CB A:THR259 3.4 15.4 1.0
CD A:GLU426 3.4 17.0 1.0
C A:TYR262 3.4 17.6 1.0
OE1 A:GLU426 3.9 17.7 1.0
CA A:THR259 3.9 16.9 1.0
N A:TYR262 4.0 17.1 1.0
CB A:ASP256 4.2 16.7 1.0
CA A:PRO263 4.2 17.4 1.0
N A:PRO263 4.3 16.8 1.0
N A:PRO260 4.3 16.6 1.0
N A:ALA264 4.3 16.2 1.0
CG A:GLU423 4.3 17.1 1.0
CA A:TYR262 4.3 17.4 1.0
C A:PRO263 4.4 16.8 1.0
N A:ASP256 4.4 16.8 1.0
O A:ASP256 4.5 17.6 1.0
N A:GLY261 4.5 16.5 1.0
CA A:PRO260 4.5 17.4 1.0
O A:ALA254 4.6 18.7 1.0
N A:THR259 4.6 16.6 1.0
CG A:GLU426 4.7 15.6 1.0
CG2 A:THR259 4.7 17.1 1.0
C A:PRO260 4.7 18.2 1.0
OD2 A:ASP256 4.7 18.4 1.0
CB A:ALA264 4.8 18.4 1.0
CA A:ASP256 4.9 16.9 1.0
CB A:GLU426 4.9 16.6 1.0
C A:GLY261 4.9 19.0 1.0
CG A:ASP256 5.0 18.0 1.0

Reference:

K.Hlouchova, C.Barinka, J.Konvalinka, J.Lubkowski. Structural Insight Into the Evolutionary and Pharmacologic Homology of Glutamate Carboxypeptidases II and III Febs J. V. 276 4448 2009.
ISSN: ISSN 1742-464X
PubMed: 19678840
DOI: 10.1111/J.1742-4658.2009.07152.X
Page generated: Sat Dec 12 04:11:28 2020

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