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Crystal structure of cuticle-degrading protease from paecilomyces lilacinus (PL646)
Analyse Crystal structure of cuticle-degrading protease from paecilomyces lilacinus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3F7O
- Type
- protein
- Length
- 576 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Serine protease; (ALA)(ALA)(PRO)(VAL)
- EC
- 3.4.21.-
- UniProt
- Q01471
- Ligands
- HMB, CA
- Pockets
- 1 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 27% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Serine protease (EC 3.4.21.-) | protein | 284 | 27% helix, 25% strand | Q01471 |
| X, Y | (ALA)(ALA)(PRO)(VAL) | protein | 4 | 0% helix, 50% strand | — |
Ligands and binding sites
- HMB · (4S)-4-hydroxy-4-methoxybutanoic acid · ligand · 2 copies · chains A, X, B, Y
- CA · Calcium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 365 | 0.65 | 0.79 | 45 | empty |
Interfaces
3 interfaces between chains.
- B–Y · 350 Ų buried · 11 hydrogen bonds · protein-protein
- A–X · 345 Ų buried · 12 hydrogen bonds · protein-protein
- A–B · 196 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 3F7O · Crystal structure of Cuticle-Degrading Protease from Paecilomyces lilacinus (PL646) · the same entry in another collection · chain A against A, TM-score 1.00
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 Q01471
- Elsewhere: RCSB PDB 3F7O · PDBe 3F7O · UniProt Q01471
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