MolNFT v1 · #74812 · protein
Radiation damage study of thermolysin - 100K structure a (0.1 mgy)
3P7P: “Radiation damage study of thermolysin - 100K structure a (0.1 mgy)”. X-ray diffraction, 2 ligands (CA, ZN), 2 pockets (best druggability 0.42). MolNFT v1 #74812 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3P7P
- 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
- CA, ZN
- Pockets
- 2 · best druggability 0.42
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E | Thermolysin (EC 3.4.24.27) | protein | 316 | 41% 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 | 60 | 0.42 | 0.81 | 15 | empty |
| 2 | 56 | 0.37 | 0.79 | 16 | empty |
Compared structures
- 3P7P · Radiation damage study of thermolysin - 100K structure A (0.1 MGy) · 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 3P7P · PDBe 3P7P · UniProt P00800
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