MolNFT v1 · #80097 · protein
The binding of L-valyl-L-tryptophan to crystalline thermolysin illustrates the mode of interaction of a product of peptide hydrolysis
3TMN: “The binding of L-valyl-L-tryptophan to crystalline thermolysin illustrates the mode of interaction of a…”. X-ray diffraction. MolNFT v1 #80097 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3TMN
- Type
- protein
- Length
- 318 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P00800
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E | — | protein | 318 | — | P00800 |
Compared structures
- 3TMN · The binding of L-valyl-L-tryptophan to crystalline thermolysin illustrates the mode of… · 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 3TMN · PDBe 3TMN · UniProt P00800
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