Research workbench
Structure of mature cpaf complexed with lactacystin
Analyse Structure of mature cpaf complexed with lactacystin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3DPM
- Type
- protein
- Length
- 1,044 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein CT_858
- UniProt
- O84866
- Ligands
- LAS
- Pockets
- 10 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Protein CT_858 | protein | 522 | 35% helix, 22% strand | O84866 |
Ligands and binding sites
- LAS · N-acetyl-S-({(2R,3S,4R)-3-hydroxy-2-[(1S)-1-hydroxy-2-methylpropyl]-4-methyl-5-oxopyrrolidin-2-yl}carbonyl)cysteine · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 629 | 0.72 | 0.79 | 64 | empty |
| 2 | 617 | 0.71 | 0.79 | 45 | empty |
| 3 | 200 | 0.65 | 0.84 | 39 | empty |
| 4 | 216 | 0.62 | 0.82 | 38 | empty |
| 5 | 267 | 0.54 | 0.76 | 37 | LAS |
Interfaces
1 interface between chains.
- A–B · 2355 Ų buried · 27 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent (covalent ligand).
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 O84866
- Elsewhere: RCSB PDB 3DPM · PDBe 3DPM · UniProt O84866
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.