Atomistry » Chlorine » PDB 2pg4-2pwr » 2pvv
Atomistry »
  Chlorine »
    PDB 2pg4-2pwr »
      2pvv »

Chlorine in PDB 2pvv: Structure of Human Glutamate Carboxypeptidase II (Gcpii) in Complex with L-Serine-O-Sulfate

Enzymatic activity of Structure of Human Glutamate Carboxypeptidase II (Gcpii) in Complex with L-Serine-O-Sulfate

All present enzymatic activity of Structure of Human Glutamate Carboxypeptidase II (Gcpii) in Complex with L-Serine-O-Sulfate:
3.4.17.21;

Protein crystallography data

The structure of Structure of Human Glutamate Carboxypeptidase II (Gcpii) in Complex with L-Serine-O-Sulfate, PDB code: 2pvv 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 / 2.11
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 101.617, 130.220, 158.975, 90.00, 90.00, 90.00
R / Rfree (%) 17.4 / 21.2

Other elements in 2pvv:

The structure of Structure of Human Glutamate Carboxypeptidase II (Gcpii) in Complex with L-Serine-O-Sulfate 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 Structure of Human Glutamate Carboxypeptidase II (Gcpii) in Complex with L-Serine-O-Sulfate (pdb code 2pvv). 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 Structure of Human Glutamate Carboxypeptidase II (Gcpii) in Complex with L-Serine-O-Sulfate, PDB code: 2pvv:

Chlorine binding site 1 out of 1 in 2pvv

Go back to Chlorine Binding Sites List in 2pvv
Chlorine binding site 1 out of 1 in the Structure of Human Glutamate Carboxypeptidase II (Gcpii) in Complex with L-Serine-O-Sulfate


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of Human Glutamate Carboxypeptidase II (Gcpii) in Complex with L-Serine-O-Sulfate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1754

b:21.0
occ:1.00
 NH1 A:ARG536 3.0 6.2 0.3
O A:HOH1789 3.2 21.8 1.0
ND2 A:ASN451 3.3 18.2 1.0
NE A:ARG534 3.3 25.7 1.0
NH1 A:ARG534 3.4 24.7 1.0
N A:ASP453 3.4 18.8 1.0
CB A:ASP453 3.7 18.6 1.0
CZ A:ARG534 3.8 25.5 1.0
CB A:ARG534 3.8 20.6 1.0
NH2 A:ARG580 4.0 17.6 1.0
CA A:ASP453 4.0 19.9 1.0
CZ A:ARG536 4.0 14.8 0.3
CB A:ASN451 4.1 17.8 1.0
CG A:ASN451 4.1 17.0 1.0
N A:ALA452 4.2 18.6 1.0
C A:ASP453 4.2 19.5 1.0
CD A:ARG536 4.3 19.4 0.3
C A:ASN451 4.3 18.5 1.0
O A:ASP453 4.4 19.3 1.0
CD A:ARG534 4.4 25.5 1.0
C A:ALA452 4.4 19.1 1.0
CD A:ARG536 4.5 30.4 0.7
CA A:ALA452 4.5 18.6 1.0
CG A:ARG534 4.5 21.1 1.0
O A:ASN451 4.6 18.4 1.0
NE A:ARG536 4.6 17.2 0.3
CZ A:ARG580 4.8 19.9 1.0
O A:SER454 4.8 19.4 1.0
NE A:ARG536 4.9 30.5 0.7
CA A:ASN451 4.9 18.2 1.0
OD1 A:ASN519 4.9 20.4 1.0
N A:SER454 4.9 19.0 1.0
NH2 A:ARG536 4.9 20.1 0.3
CG A:ASN519 4.9 18.7 1.0
CA A:ARG534 5.0 21.8 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 Jul 20 10:18:11 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy