MolNFT v1 · #134722 · protein
Crystal structure of cathepsin K with a covalently-linked inhibitor at 1.4 ångström resolution.
5TDI: “Crystal structure of cathepsin K with a covalently-linked inhibitor at 1.4 ångström resolution.”. X-ray diffraction, 1 ligand (7AS). MolNFT v1 #134722 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5TDI
- 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
- 7AS
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cathepsin K (EC 3.4.22.38) | protein | 215 | 29% helix, 23% strand | P43235 |
Ligands and binding sites
- 7AS · 4-fluoro-N-{1-[(Z)-iminomethyl]cyclopropyl}-N~2~-{(1S)-2,2,2-trifluoro-1-[4'-(methylsulfonyl)[1,1'-biphenyl]-4-yl]ethyl}-L-leucinamide · 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
- 5TDI · Crystal structure of Cathepsin K with a covalently-linked inhibitor at 1.4 Angstrom… · 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 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 P43235
- Elsewhere: RCSB PDB 5TDI · PDBe 5TDI · UniProt P43235
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