Research workbench
Structure of a hypothetical protease
Analyse Structure of a hypothetical protease in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6J91
- Type
- protein
- Length
- 258 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Small vasohibin-binding protein; Tubulinyl-tyr carboxypeptidase 1
- EC
- 3.4.17.17
- UniProt
- Q8N300, Q7L8A9
- Pockets
- 2 · best druggability 0.50
Structure
x-ray diffraction · 2 distinct chains · 47% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Small vasohibin-binding protein | protein | 24 | 83% helix, 0% strand | Q8N300 |
| B | Tubulinyl-tyr carboxypeptidase 1 (EC 3.4.17.17) | protein | 234 | 43% helix, 21% strand | Q7L8A9 |
Pockets
2 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 | 0.50 | 0.77 | 29 | empty |
| 2 | 172 | 0.44 | 0.74 | 27 | empty |
Interfaces
1 interface between chains.
- A–B · 1088 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 modified (engineered).
Compared structures
- 6J91 · Structure of a hypothetical protease · the same entry in another collection · chain A against A, TM-score 1.00
- Q7L8A9 · AlphaFold monomer V2.0 prediction for tubulinyl-tyr carboxypeptidase 1 (Q7L8A9) · a predicted model of the same protein · chain B against A, TM-score 0.99
- Q8N300 · AlphaFold monomer V2.0 prediction for small vasohibin-binding protein (Q8N300) · a predicted model of the same protein · chain A against A, TM-score 0.73
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 Q8N300
- Every structure of UniProt Q7L8A9
- Elsewhere: RCSB PDB 6J91 · PDBe 6J91 · UniProt Q8N300 · UniProt Q7L8A9
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