Research workbench
Crystal structure of calb mutant L278M from candida antarctica
Analyse Crystal structure of calb mutant L278M from candida antarctica in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4K6H
- Type
- protein
- Length
- 639 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lipase B
- EC
- 3.1.1.3
- UniProt
- P41365
- Pockets
- 3 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lipase B (EC 3.1.1.3) | protein | 319 | 36% helix, 16% strand | P41365 |
| B | Lipase B (EC 3.1.1.3) | protein | 320 | 35% helix, 16% strand | P41365 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 7 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 463 | 0.75 | 0.84 | 67 | EDO |
| 2 | 187 | 0.58 | 0.81 | 27 | EDO |
| 3 | 58 | 0.40 | 0.81 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 433 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (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 P41365
- Elsewhere: RCSB PDB 4K6H · PDBe 4K6H · UniProt P41365
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