Research workbench
NMR solution structure of the RAS-binding domain of C-RAF-1
Analyse NMR solution structure of the RAS-binding domain of C-RAF-1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1RFA
- Type
- protein
- Length
- 78 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RAF1
- EC
- 2.7.1.-
- UniProt
- P04049
Structure
solution nmr · 1 distinct chain · 19% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RAF1 (EC 2.7.1.-) | protein | 78 | 19% helix, 27% strand | P04049 |
Compared structures
- 1RFA · NMR solution structure of the RAS-binding domain of C-RAF-1 · the same entry in another collection · chain A against A, TM-score 1.00
- P04049 · AlphaFold monomer V2.0 prediction for RAF proto-oncogene SERINE/THREONINE-protein kinase… · a predicted model of the same protein · chain A against A, TM-score 0.82
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 P04049
- Elsewhere: RCSB PDB 1RFA · PDBe 1RFA · UniProt P04049
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