MolNFT v1 · #28796 · protein
Van der waals interactions dominate hydrophobic association in a protein binding site occluded from solvent water
1YP6: “Van der waals interactions dominate hydrophobic association in a protein binding site occluded from solvent…”. X-ray diffraction. MolNFT v1 #28796 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1YP6
- Type
- protein
- Length
- 157 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P11588
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 157 | — | P11588 |
Compared structures
- 1YP6 · Van der Waals Interactions Dominate Hydrophobic Association in a Protein Binding Site… · the same entry in another collection · chain A against A, TM-score 1.00
- P11588 · AlphaFold monomer V2.0 prediction for major urinary protein 1 (P11588) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P11588
- Elsewhere: RCSB PDB 1YP6 · PDBe 1YP6 · UniProt P11588
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