Research workbench
LipC12 - Lipase from metagenomics
Analyse LipC12 - Lipase from metagenomics in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6CL4
- Type
- protein
- Length
- 290 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.64
- Source
- uncultured bacterium
- Molecule
- Lipase C12
- EC
- 3.1.1.3
- UniProt
- G1APT8
Structure
x-ray diffraction · resolution 2.64 · 1 distinct chain · 41% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lipase C12 (EC 3.1.1.3) | protein | 290 | 41% helix, 16% strand | G1APT8 |
Compared structures
- 6CL4 · LIPC12 - lipase from metagenomics · 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 G1APT8
- Elsewhere: RCSB PDB 6CL4 · PDBe 6CL4 · UniProt G1APT8
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