Research workbench
ASAP1 inactive mutant E294A, an extracellular toxic zinc metalloendopeptidase
Analyse ASAP1 inactive mutant E294A, an extracellular toxic zinc metalloendopeptidase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2X3B
- Type
- protein
- Length
- 585 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Toxic extracellular endopeptidase
- EC
- 3.4.24.39
- UniProt
- Q8GMV9
- Ligands
- ZN
- Pockets
- 6 · best druggability 0.66
Structure
x-ray diffraction · 2 distinct chains · 33% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Toxic extracellular endopeptidase (EC 3.4.24.39) | protein | 295 | 33% helix, 27% strand | Q8GMV9 |
| B | Toxic extracellular endopeptidase (EC 3.4.24.39) | protein | 290 | 33% helix, 26% strand | Q8GMV9 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 567 | 0.66 | 0.77 | 64 | empty |
| 2 | 292 | 0.60 | 0.78 | 41 | empty |
| 3 | 208 | 0.49 | 0.76 | 38 | empty |
| 4 | 184 | 0.46 | 0.75 | 32 | empty |
| 5 | 74 | 0.45 | 0.82 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 1668 Ų buried · 22 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 2X3B · AsaP1 inactive mutant E294A, an extracellular toxic zinc metalloendopeptidase · 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 Q8GMV9
- Elsewhere: RCSB PDB 2X3B · PDBe 2X3B · UniProt Q8GMV9
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