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Three-dimensional structure of 4-hydroxybenzoyl CoA thioesterase from pseudomonas sp. strain cbs-3.
Analyse Three-dimensional structure of 4-hydroxybenzoyl CoA thioesterase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1BVQ
- Type
- protein
- Length
- 139 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (4-hydroxybenzoyl CoA thioesterase)
- EC
- 3.8.1.6
- UniProt
- P56653
Structure
x-ray diffraction · 1 distinct chain · 24% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (4-hydroxybenzoyl CoA thioesterase) (EC 3.8.1.6) | protein | 139 | 24% helix, 45% strand | P56653 |
Ligands and binding sites
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1BVQ · Three-dimensional structure of 4-hydroxybenzoyl CoA thioesterase from pseudomonas sp.… · 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 0.96
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 1BVQ · PDBe 1BVQ · UniProt P56653
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