Research workbench
Crystal structure of a silanediol protease inhibitor bound to thermolysin
Analyse Crystal structure of a silanediol protease inhibitor bound to thermolysin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1Y3G
- Type
- protein
- Length
- 318 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thermolysin
- EC
- 3.4.24.27
- UniProt
- P00800
- Ligands
- 3PL, CA, ZN
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E | Thermolysin (EC 3.4.24.27) | protein | 318 | 42% helix, 19% strand | P00800 |
Ligands and binding sites
- 3PL · 3-phenylpropanal · ligand · chains E
- CA · Calcium ion · metal · 4 copies · chains E
- ZN · Zinc ion · metal · chains E
- DMS · Dimethyl sulfoxide · additive · 2 copies · chains E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 covalent, 1 modified (covalent ligand, nonstandard).
Compared structures
- 1Y3G · Crystal Structure of a Silanediol Protease Inhibitor Bound to Thermolysin · the same entry in another collection · chain E against E, 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 P00800
- Elsewhere: RCSB PDB 1Y3G · PDBe 1Y3G · UniProt P00800
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.