MolNFT v1 · #106724 · protein
1.8 a resolution room temperature structure of thermolysin recorded using an xfel
4TNL: “1.8 a resolution room temperature structure of thermolysin recorded using an xfel”. X-ray diffraction, 2 ligands (CA, ZN), 2 pockets (best druggability 0.49). MolNFT v1 #106724 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 4TNL
- Type
- protein
- Length
- 315 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
- CA, ZN
- Pockets
- 2 · best druggability 0.49
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thermolysin (EC 3.4.24.27) | protein | 315 | 42% helix, 17% strand | P00800 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 130 | 0.49 | 0.79 | 25 | empty |
| 2 | 51 | 0.27 | 0.75 | 15 | empty |
Compared structures
- 4TNL · 1.8 A resolution room temperature structure of Thermolysin recorded using an XFEL · 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 P00800
- Elsewhere: RCSB PDB 4TNL · PDBe 4TNL · UniProt P00800
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