MolNFT v1 · #18969 · protein
NMR structure of the substrate binding domain of dnak bound to the peptide nrllltg
1Q5L: “NMR structure of the substrate binding domain of dnak bound to the peptide nrllltg”. Solution nmr. MolNFT v1 #18969 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1Q5L
- Type
- protein
- Length
- 122 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0A6Y8
Structure
solution nmr · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 115 | — | P0A6Y8 |
| B | — | protein | 7 | — | — |
Compared structures
- 1Q5L · NMR structure of the substrate binding domain of DnaK bound to the peptide NRLLLTG · the same entry in another collection · chain A against A, TM-score 1.00
- P0A6Y8 · AlphaFold monomer V2.0 prediction for chaperone protein dnak (P0A6Y8) · a predicted model of the same protein · chain A against A, TM-score 0.75
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 P0A6Y8
- Elsewhere: RCSB PDB 1Q5L · PDBe 1Q5L · UniProt P0A6Y8
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.