MolNFT v1 · #1196 · protein
Human cathepsin G
1AU8: “Human cathepsin G”. X-ray diffraction, 1 ligand (0H8), 1 pocket (best druggability 0.49). MolNFT v1 #1196 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1AU8
- Type
- protein
- Length
- 224 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cathepsin G
- EC
- 3.4.21.20
- UniProt
- P08311
- Ligands
- 0H8
- Pockets
- 1 · best druggability 0.49
Structure
x-ray diffraction · 1 distinct chain · 9% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cathepsin G (EC 3.4.21.20) | protein | 224 | 9% helix, 37% strand | P08311 |
Ligands and binding sites
- 0H8 · N-(3-carboxypropanoyl)-L-valyl-N-[(1R)-5-amino-1-phosphonopentyl]-L-prolinamide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 118 | 0.49 | 0.80 | 27 | 0H8 |
Modifications
Observed in the structure: 3 disulfide, 1 covalent (disulfide, covalent ligand).
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 1AU8 · PDBe 1AU8 · UniProt P08311
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