Research workbench
Crystal structure of arthrobacter sp. strain su 4-hydroxybenzoyl CoA thioesterase mutant E73Q complexed with 4-hydroxybenzoic acid
Analyse Crystal structure of arthrobacter sp. strain su 4-hydroxybenzoyl CoA… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3R36
- Type
- protein
- Length
- 281 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 4-hydroxybenzoyl-CoA thioesterase
- EC
- 3.1.2.23
- UniProt
- Q04416
- Ligands
- PHB
- Pockets
- 2 · best druggability 0.68
Structure
x-ray diffraction · 2 distinct chains · 25% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | 4-hydroxybenzoyl-CoA thioesterase (EC 3.1.2.23) | protein | 140 | 24% helix, 43% strand | Q04416 |
| A | 4-hydroxybenzoyl-CoA thioesterase (EC 3.1.2.23) | protein | 141 | 26% helix, 43% strand | Q04416 |
Ligands and binding sites
- PHB · P-hydroxybenzoic acid · ligand · 2 copies · chains B, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 277 | 0.68 | 0.83 | 42 | PHB |
| 2 | 230 | 0.67 | 0.84 | 33 | PHB |
Interfaces
1 interface between chains.
- B–A · 1607 Ų buried · 37 hydrogen bonds · protein-protein
Compared structures
- 3R36 · Crystal structure of Arthrobacter sp. strain SU 4-hydroxybenzoyl CoA thioesterase mutant… · the same entry in another collection · chain B against B, TM-score 1.00
- Q04416 · AlphaFold monomer V2.0 prediction for 4-hydroxybenzoyl-CoA thioesterase (Q04416) · a predicted model of the same protein · chain B 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 Q04416
- Elsewhere: RCSB PDB 3R36 · PDBe 3R36 · UniProt Q04416
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