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Chlorine in PDB 6czs: Crystal Structure of Human Pro-Cathepsin H C26S Mutant

Enzymatic activity of Crystal Structure of Human Pro-Cathepsin H C26S Mutant

All present enzymatic activity of Crystal Structure of Human Pro-Cathepsin H C26S Mutant:
3.4.22.16;

Protein crystallography data

The structure of Crystal Structure of Human Pro-Cathepsin H C26S Mutant, PDB code: 6czs was solved by X.Huang, Y.Hao, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.12 / 1.66
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 98.242, 98.242, 106.586, 90.00, 90.00, 120.00
R / Rfree (%) 18.1 / 20.9

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Human Pro-Cathepsin H C26S Mutant (pdb code 6czs). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of Human Pro-Cathepsin H C26S Mutant, PDB code: 6czs:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 6czs

Go back to Chlorine Binding Sites List in 6czs
Chlorine binding site 1 out of 2 in the Crystal Structure of Human Pro-Cathepsin H C26S Mutant


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Human Pro-Cathepsin H C26S Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl414

b:55.8
occ:1.00
N A:ASN292 3.3 39.7 1.0
O A:HOH689 3.3 49.1 1.0
CA A:ASN292 4.1 36.9 1.0
OD1 A:ASN292 4.2 45.0 1.0
CA A:LYS291 4.2 28.5 1.0
C A:LYS291 4.3 28.7 1.0
CD A:LYS291 4.4 51.2 1.0
O A:GLU290 4.7 24.9 1.0
NZ A:LYS291 4.8 55.5 1.0
N A:GLY293 4.9 29.6 1.0
CG A:ASN292 4.9 46.3 1.0
CG A:LYS291 5.0 40.1 1.0

Chlorine binding site 2 out of 2 in 6czs

Go back to Chlorine Binding Sites List in 6czs
Chlorine binding site 2 out of 2 in the Crystal Structure of Human Pro-Cathepsin H C26S Mutant


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Human Pro-Cathepsin H C26S Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl415

b:53.4
occ:1.00
O A:HOH876 3.4 42.8 1.0
NH1 A:ARG263 3.5 19.4 1.0
OG1 A:THR264 3.6 19.1 1.0
O A:HOH646 3.9 39.8 1.0
NH2 A:ARG263 4.1 19.4 1.0
CB A:THR264 4.2 15.9 1.0
CE A:MET309 4.2 24.9 1.0
CZ A:ARG263 4.2 21.6 1.0
CG A:MET309 4.4 15.5 1.0
CB A:MET309 4.8 15.3 1.0

Reference:

Y.Hao, W.Purtha, C.Cortesio, H.Rui, Y.Gu, H.Chen, E.A.Sickmier, P.Manzanillo, X.Huang. Crystal Structures of Human Procathepsin H. Plos One V. 13 00374 2018.
ISSN: ESSN 1932-6203
PubMed: 30044821
DOI: 10.1371/JOURNAL.PONE.0200374
Page generated: Sat Jul 12 12:37:24 2025

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