Research workbench
Crystal structure of E. COLI lysophospholiase L1/ACYL-CoA thioesterase I/PROTEASE I L109P mutant
Analyse Crystal structure of E. COLI lysophospholiase L1/ACYL-CoA thioesterase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1JRL
- Type
- protein
- Length
- 178 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acyl-CoA thioesterase I
- EC
- 3.1.2.-, 3.1.1.5
- UniProt
- P29679
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.50
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acyl-CoA thioesterase I (EC 3.1.2.-, 3.1.1.5) | protein | 178 | 51% helix, 15% strand | P29679 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 105 | 0.50 | 0.81 | 21 | empty |
Compared structures
- 1JRL · Crystal structure of E. coli Lysophospholiase L1/Acyl-CoA Thioesterase I/Protease I L109P… · the same entry in another collection · 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 P29679
- Elsewhere: RCSB PDB 1JRL · PDBe 1JRL · UniProt P29679
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