MolNFT v1 · #18940 · protein
Structural studies of PHE256TRP of human salivary alpha-amylase: implications for the role of a conserved water molecule and its associated chain in enzyme activity
1Q4N: “Structural studies of PHE256TRP of human salivary alpha-amylase: implications for the role of a conserved…”. X-ray diffraction. MolNFT v1 #18940 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1Q4N
- Type
- protein
- Length
- 496 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P04745
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | — | protein | 496 | — | P04745 |
Compared structures
- 1Q4N · Structural studies of Phe256Trp of human salivary alpha-amylase: implications for the… · the same entry in another collection · chain X against X, 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 P04745
- Elsewhere: RCSB PDB 1Q4N · PDBe 1Q4N · UniProt P04745
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