Atomistry » Chlorine » PDB 2dct-2dxa » 2djg
Atomistry »
  Chlorine »
    PDB 2dct-2dxa »
      2djg »

Chlorine in PDB 2djg: Re-Determination of the Native Structure of Human Dipeptidyl Peptidase I (Cathepsin C)

Enzymatic activity of Re-Determination of the Native Structure of Human Dipeptidyl Peptidase I (Cathepsin C)

All present enzymatic activity of Re-Determination of the Native Structure of Human Dipeptidyl Peptidase I (Cathepsin C):
3.4.14.1;

Protein crystallography data

The structure of Re-Determination of the Native Structure of Human Dipeptidyl Peptidase I (Cathepsin C), PDB code: 2djg was solved by A.Molgaard, J.Arnau, C.Lauritzen, S.Larsen, G.Petersen, J.Pedersen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.04 / 2.05
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 87.479, 88.680, 114.350, 90.00, 90.00, 90.00
R / Rfree (%) 17.4 / 22.1

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Re-Determination of the Native Structure of Human Dipeptidyl Peptidase I (Cathepsin C) (pdb code 2djg). 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 Re-Determination of the Native Structure of Human Dipeptidyl Peptidase I (Cathepsin C), PDB code: 2djg:

Chlorine binding site 1 out of 1 in 2djg

Go back to Chlorine Binding Sites List in 2djg
Chlorine binding site 1 out of 1 in the Re-Determination of the Native Structure of Human Dipeptidyl Peptidase I (Cathepsin C)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Re-Determination of the Native Structure of Human Dipeptidyl Peptidase I (Cathepsin C) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl500

b:19.2
occ:1.00
OH B:TYR323 3.2 20.7 1.0
O C:HOH87 3.3 26.8 1.0
N B:TYR280 3.3 16.9 1.0
O C:HOH185 3.4 32.4 1.0
CD B:PRO279 3.6 19.4 1.0
CB B:PHE278 3.6 18.3 1.0
CE1 B:TYR323 3.6 17.9 1.0
CB B:TYR280 3.6 16.2 1.0
N B:PRO279 3.7 17.9 1.0
CG2 C:VAL431 3.7 20.9 1.0
CZ B:TYR323 3.9 17.7 1.0
CD2 B:PHE278 3.9 21.4 1.0
C B:PHE278 4.0 18.6 1.0
CD1 C:ILE429 4.0 17.4 1.0
CA B:TYR280 4.0 16.6 1.0
CA B:PHE278 4.1 18.0 1.0
C B:PRO279 4.2 18.1 1.0
CG1 C:ILE429 4.2 17.5 1.0
CG B:PHE278 4.2 19.8 1.0
CA B:PRO279 4.3 18.9 1.0
CB B:PRO279 4.3 19.1 1.0
CG B:PRO279 4.5 17.3 1.0
O B:PHE278 4.8 19.0 1.0
CD1 B:TYR323 4.8 16.7 1.0
CG2 A:ILE63 4.9 16.7 1.0
O C:ILE429 4.9 17.0 1.0
CB C:VAL431 5.0 19.6 1.0
CG B:TYR280 5.0 14.3 1.0

Reference:

A.Molgaard, J.Arnau, C.Lauritzen, S.Larsen, G.Petersen, J.Pedersen. The Crystal Structure of Human Dipeptidyl Peptidase I (Cathepsin C) in Complex with the Inhibitor Gly-Phe-CHN2 Biochem.J. V. 401 645 2007.
ISSN: ISSN 0264-6021
PubMed: 17020538
DOI: 10.1042/BJ20061389
Page generated: Sat Jul 20 06:34:28 2024

Last articles

Zn in 9MJ5
Zn in 9HNW
Zn in 9G0L
Zn in 9FNE
Zn in 9DZN
Zn in 9E0I
Zn in 9D32
Zn in 9DAK
Zn in 8ZXC
Zn in 8ZUF
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy