Research workbench
Fully activated a. thaliana legumain isoform gamma in complex with ac- yvad-cmk
Analyse Fully activated a. thaliana legumain isoform gamma in complex with ac- yvad-cmk in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5OBT
- Type
- protein
- Length
- 564 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q39119
- Ligands
- SNN, ACE, 0QE
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 227 | — | Q39119 |
| E, F | — | protein | 50 | — | Q39119 |
| C, D | — | protein | 4 | — | — |
| B | — | protein | 229 | — | Q39119 |
Ligands and binding sites
- SNN · L-3-aminosuccinimide · ligand · 2 copies · chains A, C, B, D
- ACE · Acetyl group · ligand · 2 copies · chains A, E, C, B, D, F
- 0QE · Chloromethane · ion · 2 copies · chains A, C, F, E, B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5OBT · Fully activated A. thaliana legumain isoform gamma in complex with Ac-YVAD-CMK · the same entry in another collection · chain C against C, TM-score 1.00
- Q39119 · AlphaFold monomer V2.0 prediction for vacuolar-processing enzyme gamma-isozyme (Q39119) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q39119
- Elsewhere: RCSB PDB 5OBT · PDBe 5OBT · UniProt Q39119
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