Research workbench
Human acyl-coenzyme a thioesterase 4
Analyse Human acyl-coenzyme a thioesterase 4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3K2I
- Type
- protein
- Length
- 810 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acyl-coenzyme a thioesterase 4
- EC
- 3.1.2.2
- UniProt
- Q8N9L9
- Ligands
- NI, CL
- Pockets
- 9 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 20% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Acyl-coenzyme a thioesterase 4 (EC 3.1.2.2) | protein | 405 | 20% helix, 32% strand | Q8N9L9 |
Ligands and binding sites
- NI · Nickel (II) ion · metal · 2 copies · chains A, B
- CL · Chloride ion · ion · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1051 | 0.86 | 0.87 | 98 | NI, CL |
| 2 | 394 | 0.74 | 0.84 | 53 | CL |
| 3 | 142 | 0.70 | 0.89 | 30 | CL |
| 4 | 261 | 0.60 | 0.79 | 28 | empty |
| 5 | 234 | 0.58 | 0.79 | 35 | empty |
Interfaces
1 interface between chains.
- A–B · 1540 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
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 Q8N9L9
- Elsewhere: RCSB PDB 3K2I · PDBe 3K2I · UniProt Q8N9L9
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