Research workbench
Lcp-embedded proteinase K treated with lipase
Analyse Lcp-embedded proteinase K treated with lipase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6PQ4
- Type
- protein
- Length
- 279 residues
- Chains
- 1
- Method
- electron crystallography
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Proteinase K
- EC
- 3.4.21.64
- UniProt
- P06873
- Ligands
- CA, NO3
- Pockets
- 1 · best druggability 0.39
Structure
electron crystallography · 1 distinct chain · 28% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Proteinase K (EC 3.4.21.64) | protein | 279 | 28% helix, 24% strand | P06873 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 90 | 0.39 | 0.77 | 27 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 6PQ4 · LCP-embedded Proteinase K treated with lipase · 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 P06873
- Elsewhere: RCSB PDB 6PQ4 · PDBe 6PQ4 · UniProt P06873
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