Research workbench
Structure of esta from clostridium botulinum
Analyse Structure of esta from clostridium botulinum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5AH1
- Type
- protein
- Length
- 427 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Triacylglycerol lipase
- EC
- 3.1.1.3
- UniProt
- A7FSB2
- Ligands
- K, ZN
- Pockets
- 4 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Triacylglycerol lipase (EC 3.1.1.3) | protein | 427 | 36% helix, 15% strand | A7FSB2 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 217 | 0.84 | 0.97 | 32 | empty |
| 2 | 165 | 0.61 | 0.83 | 24 | empty |
| 3 | 71 | 0.33 | 0.75 | 20 | K |
| 4 | 55 | 0.27 | 0.74 | 16 | K |
Compared structures
- 5AH1 · Structure of EstA from Clostridium botulinum · 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 A7FSB2
- Elsewhere: RCSB PDB 5AH1 · PDBe 5AH1 · UniProt A7FSB2
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