Research workbench
X-ray crystal structure of 4-hydroxybenzoyl CoA thioesterase complexed with 4-hydroxybenzyl CoA
Analyse X-ray crystal structure of 4-hydroxybenzoyl CoA thioesterase complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1LO8
- Type
- protein
- Length
- 140 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 4-hydroxybenzoyl-CoA thioesterase
- EC
- 3.1.2.23
- UniProt
- P56653
- Ligands
- 4CA
Structure
x-ray diffraction · 1 distinct chain · 24% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 4-hydroxybenzoyl-CoA thioesterase (EC 3.1.2.23) | protein | 140 | 24% helix, 44% strand | P56653 |
Ligands and binding sites
- 4CA · 4-hydroxybenzyl coenzyme A · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1LO8 · X-ray crystal structure of 4-hydroxybenzoyl CoA thioesterase complexed with… · the same entry in another collection · chain A against A, TM-score 1.00
- P56653 · AlphaFold monomer V2.0 prediction for 4-hydroxybenzoyl-CoA thioesterase (P56653) · a predicted model of the same protein · 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 P56653
- Elsewhere: RCSB PDB 1LO8 · PDBe 1LO8 · UniProt P56653
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.