Research workbench
Structure determination of the RAS-binding domain of the ral-specific guanine nucleotide exchange factor rlf, NMR, 10 structures
Analyse Structure determination of the RAS-binding domain of the ral-specific guanine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1RLF
- Type
- protein
- Length
- 90 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Rlf
- UniProt
- Q61193
Structure
solution nmr · 1 distinct chain · 13% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Rlf | protein | 90 | 13% helix, 30% strand | Q61193 |
Compared structures
- 1RLF · Structure determination of the RAS-binding domain of the ral-specific guanine nucleotide… · the same entry in another collection · chain A against A, TM-score 1.00
- Q61193 · AlphaFold monomer V2.0 prediction for ral guanine nucleotide dissociation stimulator-like… · a predicted model of the same protein · chain A against A, TM-score 0.56
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 Q61193
- Elsewhere: RCSB PDB 1RLF · PDBe 1RLF · UniProt Q61193
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