Research workbench
1.8 ångströms refined structure of the lipase from geotrichum candidum
Analyse 1.8 ångströms refined structure of the lipase from geotrichum candidum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1THG
- Type
- protein
- Length
- 544 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lipase 2
- EC
- 3.1.1.3
- UniProt
- P22394
- Ligands
- NAG, NDG
- Pockets
- 3 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lipase 2 (EC 3.1.1.3) | protein | 544 | 39% helix, 16% strand | P22394 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A
- NDG · 2-acetamido-2-deoxy-alpha-D-glucopyranose · sugar · chains A
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 | 216 | 0.83 | 0.97 | 54 | empty |
| 2 | 136 | 0.53 | 0.81 | 33 | empty |
| 3 | 52 | 0.27 | 0.74 | 12 | empty |
Modifications
Observed in the structure: 3 glycan, 2 disulfide, 1 modified (disulfide, N-glycosylation, O-glycosylation, cyclization).
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 P22394
- Elsewhere: RCSB PDB 1THG · PDBe 1THG · UniProt P22394
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