MolNFT v1 · #1345 · protein
Crystal structure of cysteine protease human cathepsin K in complex with a covalent benzyloxybenzoylcarbohydrazide inhibitor
1AYW: “Crystal structure of cysteine protease human cathepsin K in complex with a covalent…”. X-ray diffraction, 1 ligand (IN3). MolNFT v1 #1345 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1AYW
- Type
- protein
- Length
- 215 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cathepsin K
- EC
- 3.4.22.38
- UniProt
- P43235
- Ligands
- IN3
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cathepsin K (EC 3.4.22.38) | protein | 215 | 29% helix, 21% strand | P43235 |
Ligands and binding sites
- IN3 · 1-(N-benzyloxycarbonyl-L-leucinyl)-5-(3-benzyloxy benzoyl)carbohydrazide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 3 disulfide, 1 covalent (disulfide, covalent ligand).
Compared structures
- 1AYW · Crystal structure of cysteine protease human cathepsin K in complex with a covalent… · the same entry in another collection · chain A against A, TM-score 1.00
- P43235 · AlphaFold monomer V2.0 prediction for cathepsin K (P43235) · 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 P43235
- Elsewhere: RCSB PDB 1AYW · PDBe 1AYW · UniProt P43235
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