Research workbench
Structure of candida antarctica lipase B mutant
Analyse Structure of candida antarctica lipase B mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ISP
- Type
- protein
- Length
- 1,270 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lipase B
- EC
- 3.1.1.3
- UniProt
- P41365
- Ligands
- CPQ, CA
- Pockets
- 5 · best druggability 0.81
Structure
x-ray diffraction · 3 distinct chains · 36% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| D, B | Lipase B (EC 3.1.1.3) | protein | 317 | 36% helix, 16% strand | P41365 |
| A | Lipase B (EC 3.1.1.3) | protein | 317 | 36% helix, 16% strand | P41365 |
| C | Lipase B (EC 3.1.1.3) | protein | 319 | 35% helix, 16% strand | P41365 |
Ligands and binding sites
- CPQ · N,N-bis(3-D-gluconamidopropyl)deoxycholamide · ligand · 11 copies · chains D, A, C, B
- CA · Calcium ion · metal · 2 copies · chains D, A, C, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1169 | 0.81 | 0.82 | 129 | CA, CPQ |
| 2 | 1192 | 0.80 | 0.81 | 136 | CPQ |
| 3 | 528 | 0.71 | 0.80 | 54 | empty |
| 4 | 75 | 0.33 | 0.74 | 14 | empty |
| 5 | 55 | 0.32 | 0.76 | 15 | empty |
Interfaces
3 interfaces between chains.
- A–C · 715 Ų buried · 4 hydrogen bonds · protein-protein
- C–B · 602 Ų buried · 0 hydrogen bonds · protein-protein
- D–A · 597 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 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 6ISP · PDBe 6ISP · UniProt P41365
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