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Chlorine in PDB 2or4: A High Resolution Crystal Structure of Human Glutamate Carboxypeptidase II in Complex with Quisqualic Acid

Enzymatic activity of A High Resolution Crystal Structure of Human Glutamate Carboxypeptidase II in Complex with Quisqualic Acid

All present enzymatic activity of A High Resolution Crystal Structure of Human Glutamate Carboxypeptidase II in Complex with Quisqualic Acid:
3.4.17.21;

Protein crystallography data

The structure of A High Resolution Crystal Structure of Human Glutamate Carboxypeptidase II in Complex with Quisqualic Acid, PDB code: 2or4 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 / 1.62
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 102.007, 130.437, 159.508, 90.00, 90.00, 90.00
R / Rfree (%) 18.4 / 21.9

Other elements in 2or4:

The structure of A High Resolution Crystal Structure of Human Glutamate Carboxypeptidase II in Complex with Quisqualic Acid also contains other interesting chemical elements:

Calcium (Ca) 1 atom
Zinc (Zn) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the A High Resolution Crystal Structure of Human Glutamate Carboxypeptidase II in Complex with Quisqualic Acid (pdb code 2or4). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the A High Resolution Crystal Structure of Human Glutamate Carboxypeptidase II in Complex with Quisqualic Acid, PDB code: 2or4:

Chlorine binding site 1 out of 1 in 2or4

Go back to Chlorine Binding Sites List in 2or4
Chlorine binding site 1 out of 1 in the A High Resolution Crystal Structure of Human Glutamate Carboxypeptidase II in Complex with Quisqualic Acid


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of A High Resolution Crystal Structure of Human Glutamate Carboxypeptidase II in Complex with Quisqualic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1754

b:21.4
occ:1.00
 ND2 A:ASN451 3.2 17.4 1.0
O A:HOH1821 3.2 21.5 1.0
NE A:ARG534 3.3 22.5 1.0
NH2 A:ARG536 3.3 10.5 0.3
NH1 A:ARG534 3.4 25.4 1.0
N A:ASP453 3.4 17.0 1.0
CZ A:ARG534 3.8 24.3 1.0
CB A:ASP453 3.8 18.6 1.0
CB A:ARG534 3.9 19.4 1.0
NH2 A:ARG580 4.0 18.2 1.0
CA A:ASP453 4.0 16.6 1.0
CB A:ASN451 4.0 16.0 1.0
CG A:ASN451 4.1 16.1 1.0
CZ A:ARG536 4.2 17.6 0.3
N A:ALA452 4.2 17.3 1.0
C A:ASP453 4.3 17.9 1.0
CD A:ARG536 4.3 26.6 0.7
C A:ASN451 4.3 17.7 1.0
C A:ALA452 4.4 17.8 1.0
CD A:ARG534 4.4 22.3 1.0
NE A:ARG536 4.4 17.4 0.3
O A:ASP453 4.4 16.9 1.0
CA A:ALA452 4.4 16.9 1.0
O A:ASN451 4.5 18.5 1.0
CG A:ARG534 4.5 19.2 1.0
NE A:ARG536 4.7 28.3 0.7
O A:SER454 4.8 19.9 1.0
CZ A:ARG580 4.8 18.1 1.0
CA A:ASN451 4.9 15.7 1.0
CA A:ARG534 4.9 18.0 1.0
N A:SER454 4.9 17.1 1.0
O A:ALA535 4.9 18.1 1.0

Reference:

C.Barinka, M.Rovenska, P.Mlcochova, K.Hlouchova, A.Plechanovova, P.Majer, T.Tsukamoto, B.S.Slusher, J.Konvalinka, J.Lubkowski. Structural Insight Into the Pharmacophore Pocket of Human Glutamate Carboxypeptidase II. J.Med.Chem. V. 50 3267 2007.
ISSN: ISSN 0022-2623
PubMed: 17567119
DOI: 10.1021/JM070133W
Page generated: Sat Dec 12 09:13:53 2020

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