Research workbench
NMR structure of the substrate binding domain of dnak bound to the peptide nrllltg
Analyse NMR structure of the substrate binding domain of dnak bound to the peptide… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1Q5L
- Type
- protein
- Length
- 122 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chaperone protein dnak; Peptide nrllltg
- UniProt
- P0A6Y8
Structure
solution nmr · 2 distinct chains · 0% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chaperone protein dnak | protein | 115 | 0% helix, 39% strand | P0A6Y8 |
| B | Peptide nrllltg | protein | 7 | 0% helix, 0% strand | — |
Interfaces
1 interface between chains.
- A–B · 538 Ų buried · 4 hydrogen bonds · protein-protein
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
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