Research workbench
Human start domain of acyl-coenzyme a thioesterase 11 (ACOT11) bound to myristic acid
Analyse Human start domain of acyl-coenzyme a thioesterase 11 (ACOT11) bound to… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6VVQ
- Type
- protein
- Length
- 920 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acyl-coenzyme a thioesterase 11
- EC
- 3.1.2.-, 3.1.2.2
- UniProt
- Q8WXI4
- Ligands
- MYR
- Pockets
- 10 · best druggability 0.83
Structure
x-ray diffraction · 4 distinct chains · 31% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acyl-coenzyme a thioesterase 11 (EC 3.1.2.-, 3.1.2.2) | protein | 237 | 31% helix, 32% strand | Q8WXI4 |
| B | Acyl-coenzyme a thioesterase 11 (EC 3.1.2.-, 3.1.2.2) | protein | 229 | 30% helix, 34% strand | Q8WXI4 |
| C | Acyl-coenzyme a thioesterase 11 (EC 3.1.2.-, 3.1.2.2) | protein | 234 | 32% helix, 34% strand | Q8WXI4 |
| D | Acyl-coenzyme a thioesterase 11 (EC 3.1.2.-, 3.1.2.2) | protein | 220 | 30% helix, 36% strand | Q8WXI4 |
Ligands and binding sites
- MYR · Myristic acid · ligand · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 201 | 0.83 | 0.96 | 27 | MYR |
| 2 | 197 | 0.82 | 0.96 | 28 | empty |
| 3 | 166 | 0.82 | 0.96 | 27 | empty |
| 4 | 385 | 0.76 | 0.86 | 46 | empty |
| 5 | 480 | 0.69 | 0.80 | 67 | empty |
Interfaces
4 interfaces between chains.
- A–B · 942 Ų buried · 11 hydrogen bonds · protein-protein
- A–C · 805 Ų buried · 15 hydrogen bonds · protein-protein
- C–D · 405 Ų buried · 2 hydrogen bonds · protein-protein
- B–C · 49 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 6VVQ · Human START domain of Acyl-coenzyme A thioesterase 11 (ACOT11) bound to Myristic Acid · the same entry in another collection · chain D against D, TM-score 1.00
- Q8WXI4 · AlphaFold monomer V2.0 prediction for acyl-coenzyme a thioesterase 11 (Q8WXI4) · a predicted model of the same protein · chain D against A, TM-score 0.86
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 Q8WXI4
- Elsewhere: RCSB PDB 6VVQ · PDBe 6VVQ · UniProt Q8WXI4
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