Research workbench
Crystal structure of acyl-CoA hydrolase (NP_241664.1) from bacillus halodurans at 1.66 a resolution
Analyse Crystal structure of acyl-CoA hydrolase (NP_241664.1) from bacillus halodurans… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1VPM
- Type
- protein
- Length
- 460 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acyl-CoA hydrolase
- EC
- 3.1.2.-
- UniProt
- Q9KEQ1
- Ligands
- COA, PO4
- Pockets
- 8 · best druggability 0.61
Structure
x-ray diffraction · 3 distinct chains · 30% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acyl-CoA hydrolase (EC 3.1.2.-) | protein | 155 | 30% helix, 40% strand | Q9KEQ1 |
| B | Acyl-CoA hydrolase (EC 3.1.2.-) | protein | 151 | 30% helix, 41% strand | Q9KEQ1 |
| C | Acyl-CoA hydrolase (EC 3.1.2.-) | protein | 154 | 29% helix, 39% strand | Q9KEQ1 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 361 | 0.61 | 0.77 | 52 | empty |
| 2 | 95 | 0.56 | 0.85 | 30 | empty |
| 3 | 200 | 0.44 | 0.73 | 34 | empty |
| 4 | 95 | 0.37 | 0.76 | 20 | empty |
| 5 | 51 | 0.36 | 0.80 | 16 | empty |
Interfaces
3 interfaces between chains.
- B–C · 1018 Ų buried · 14 hydrogen bonds · protein-protein
- A–C · 812 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 154 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 modified (engineered).
Compared structures
- 1VPM · Crystal structure of Acyl-CoA hydrolase (NP_241664.1) from Bacillus halodurans at 1.66 A… · the same entry in another collection · chain B against B, 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 Q9KEQ1
- Elsewhere: RCSB PDB 1VPM · PDBe 1VPM · UniProt Q9KEQ1
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