Research workbench
Crystal structure of trichoderma reesei aspartic proteinase
Analyse Crystal structure of trichoderma reesei aspartic proteinase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3C9X
- Type
- protein
- Length
- 329 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Trichoderma reesei aspartic protease
- EC
- 3.4.23.18
- UniProt
- Q2WBH2
- Pockets
- 1 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 12% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Trichoderma reesei aspartic protease (EC 3.4.23.18) | protein | 329 | 12% helix, 43% strand | Q2WBH2 |
Ligands and binding sites
- GOL · Glycerol · additive · 5 copies · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 315 | 0.56 | 0.75 | 40 | GOL |
Modifications
Observed in the structure: 1 disulfide, 1 modified (disulfide, cyclization).
Compared structures
- 3C9X · Crystal structure of Trichoderma reesei aspartic proteinase · 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 Q2WBH2
- Elsewhere: RCSB PDB 3C9X · PDBe 3C9X · UniProt Q2WBH2
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