MolNFT v1 · #22829 · protein
Thermolysin complexed with a novel glutaramide derivative, N-(1-(2(R, S)-carboxy-4-phenylbutyl) cyclopentylcarbonyl)-(S)-tryptophan
1THL: “Thermolysin complexed with a novel glutaramide derivative, N-(1-(2(R, S)-carboxy-4-phenylbutyl)…”. X-ray diffraction, 3 ligands (0DB, CA, ZN), 1 pocket (best druggability 0.44). MolNFT v1 #22829 on GenesisL1: 3D structure, binding…
- PDB
- 1THL
- Type
- protein
- Length
- 316 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
- 0DB, CA, ZN
- Pockets
- 1 · best druggability 0.44
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thermolysin (EC 3.4.24.27) | protein | 316 | 41% helix, 18% strand | P00800 |
Ligands and binding sites
- 0DB · N-({1-[(2S)-2-carboxy-4-phenylbutyl]cyclopentyl}carbonyl)-L-tryptophan · ligand · chains A
- CA · Calcium ion · metal · 4 copies · chains A
- ZN · Zinc ion · metal · 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 | 122 | 0.44 | 0.77 | 25 | 0DB |
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 P00800
- Elsewhere: RCSB PDB 1THL · PDBe 1THL · UniProt P00800
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