Research workbench
CATHEPSIN-G
Analyse CATHEPSIN-G in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1KYN
- Type
- protein
- Length
- 448 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cathepsin G
- EC
- 3.4.21.20
- UniProt
- P08311
- Ligands
- KTP
- Pockets
- 3 · best druggability 0.48
Structure
x-ray diffraction · 2 distinct chains · 7% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cathepsin G (EC 3.4.21.20) | protein | 223 | 7% helix, 31% strand | P08311 |
| B | Cathepsin G (EC 3.4.21.20) | protein | 225 | 7% helix, 31% strand | P08311 |
Ligands and binding sites
- KTP · (2-naphthalen-2-yl-1-naphthalen-1-yl-2-oxo-ethyl)-phosphonic acid · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 173 | 0.48 | 0.76 | 36 | KTP |
| 2 | 143 | 0.47 | 0.78 | 31 | KTP |
| 3 | 191 | 0.45 | 0.75 | 27 | empty |
Interfaces
1 interface between chains.
- A–B · 160 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P08311
- Elsewhere: RCSB PDB 1KYN · PDBe 1KYN · UniProt P08311
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