MolNFT v1 · #134618 · protein
Conformational sampling differences across the arrhenius plot biphasic break point at ambient temperature in the enzyme thermolysin
5T9K: “Conformational sampling differences across the arrhenius plot biphasic break point at ambient temperature in…”. X-ray diffraction, 2 ligands (CA, ZN), 2 pockets (best druggability 0.39). MolNFT v1 #134618 on GenesisL1: 3D structure…
- PDB
- 5T9K
- 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
- CA, ZN
- Pockets
- 2 · best druggability 0.39
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thermolysin (EC 3.4.24.27) | protein | 318 | 42% helix, 18% 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 | 72 | 0.39 | 0.78 | 16 | empty |
| 2 | 52 | 0.27 | 0.75 | 15 | empty |
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 5T9K · PDBe 5T9K · UniProt P00800
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