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Burkholderia cepacia lipase complexed with hexylphosphonic acid (R)-2-methyl-3-phenylpropyl ester
Analyse Burkholderia cepacia lipase complexed with hexylphosphonic acid… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1YS1
- Type
- protein
- Length
- 320 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lipase
- EC
- 3.1.1.3
- UniProt
- P22088
- Ligands
- 2HR, CA
- Pockets
- 2 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | Lipase (EC 3.1.1.3) | protein | 320 | 38% helix, 19% strand | P22088 |
Ligands and binding sites
- 2HR · Hexylphosphonic acid (R)-2-methyl-3-phenylpropyl ester · ligand · chains X
- CA · Calcium ion · metal · chains X
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 441 | 0.66 | 0.78 | 38 | 2HR |
| 2 | 55 | 0.29 | 0.75 | 25 | empty |
Modifications
Observed in the structure: 1 covalent, 1 disulfide (covalent ligand, disulfide).
Compared structures
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 P22088
- Elsewhere: RCSB PDB 1YS1 · PDBe 1YS1 · UniProt P22088
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