MolNFT v2 · #191906 · protein
Crystal structure of human Cathepsin L in complex with covalently bound MG132
7QKD: “Crystal structure of human Cathepsin L in complex with covalently bound MG132”. X-ray diffraction at 1.5, 1 ligand (ALD). MolNFT v2 #191906 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7QKD
- Type
- protein
- Length
- 876 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.5
- Source
- Homo sapiens
- UniProt
- P07711
- Ligands
- ALD
Structure
x-ray diffraction · resolution 1.5 · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, D | — | protein | 220 | — | P07711 |
| C | — | protein | 216 | — | P07711 |
Ligands and binding sites
- ALD · N-[(benzyloxy)carbonyl]-L-leucyl-N-[(2S)-1-hydroxy-4-methylpentan-2-yl]-L-leucinamide · ligand · 4 copies · chains A, B, C, D
- PEG · Di(hydroxyethyl)ether · additive · 7 copies · chains A, B, C, D
- ACT · Acetate ion · additive · chains B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- P07711 · AlphaFold monomer V2.0 prediction for procathepsin L (P07711) · a predicted model of the same protein · chain C 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 P07711
- Elsewhere: RCSB PDB 7QKD · PDBe 7QKD · UniProt P07711
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