Research workbench
Bacillus pumilus lipase a
Analyse Bacillus pumilus lipase a in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7R25
- Type
- protein
- Length
- 184 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lipase
- UniProt
- W8FKE7
- Ligands
- PO4
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lipase | protein | 184 | 40% helix, 19% strand | W8FKE7 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · chains A
- CIT · Citric acid · additive · chains A
- PPI · Propanoic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7R25 · Bacillus pumilus Lipase A · 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 W8FKE7
- Elsewhere: RCSB PDB 7R25 · PDBe 7R25 · UniProt W8FKE7
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