MolNFT v1 · #50986 · protein
Crystal structure of the catalytic domain of human fibroblast stromelysin-1 inhibited with thiadiazole inhibitor pnu-141803
2USN: “Crystal structure of the catalytic domain of human fibroblast stromelysin-1 inhibited with thiadiazole…”. X-ray diffraction, 3 ligands (IN8, ZN, CA), 1 pocket (best druggability 0.30). MolNFT v1 #50986 on GenesisL1: 3D structure…
- PDB
- 2USN
- Type
- protein
- Length
- 165 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Stromelysin-1
- EC
- 3.4.24.17
- UniProt
- P08254
- Ligands
- IN8, ZN, CA
- Pockets
- 1 · best druggability 0.30
Structure
x-ray diffraction · 1 distinct chain · 28% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Stromelysin-1 (EC 3.4.24.17) | protein | 165 | 28% helix, 18% strand | P08254 |
Ligands and binding sites
- IN8 · [2-(5-mercapto-[1,3,4]thiadiazol-2-ylcarbamoyl)-1-phenyl-ethyl]-carbamic acid benzyl ester · ligand · chains A
- ZN · Zinc ion · metal · 3 copies · chains A
- CA · Calcium ion · metal · 3 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 | 70 | 0.30 | 0.73 | 18 | IN8 |
Compared structures
- 2USN · Crystal structure of the catalytic domain of human fibroblast stromelysin-1 inhibited… · the same entry in another collection · 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 P08254
- Elsewhere: RCSB PDB 2USN · PDBe 2USN · UniProt P08254
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