MolNFT v1 · #29568 · protein
Human calpain protease core inhibited by ZLLYCH2F
1ZCM · Calpain 1, large [catalytic] subunit: “Human calpain protease core inhibited by ZLLYCH2F”. X-ray diffraction, 2 ligands (C1N, CA), 1 pocket (best druggability 0.32). MolNFT v1 #29568 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1ZCM
- Type
- protein
- Length
- 321 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calpain 1, large [catalytic] subunit
- EC
- 3.4.22.52
- UniProt
- P07384
- Ligands
- C1N, CA
- Pockets
- 1 · best druggability 0.32
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Calpain 1, large [catalytic] subunit (EC 3.4.22.52) | protein | 321 | 31% helix, 24% strand | P07384 |
Ligands and binding sites
- C1N · N-[(benzyloxy)carbonyl]leucyl-N~1~-[3-fluoro-1-(4-hydroxybenzyl)-2-oxopropyl]leucinamide · ligand · chains A
- CA · Calcium ion · metal · 2 copies · chains A
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 | 80 | 0.32 | 0.75 | 20 | C1N |
Modifications
Observed in the structure: 1 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 P07384
- Elsewhere: RCSB PDB 1ZCM · PDBe 1ZCM · UniProt P07384
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