Research workbench
Crystal structure of the active RAS protein complexed with the RAS- interacting domain of ralgds
Analyse Crystal structure of the active RAS protein complexed with the RAS- interacting… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1LFD
- Type
- protein
- Length
- 508 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q03386, P01112
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | — | protein | 87 | — | Q03386 |
| B, D | — | protein | 167 | — | P01112 |
Compared structures
- 1LFD · Crystal structure of the active RAS protein complexed with the RAS-interacting domain of… · the same entry in another collection · chain A against A, TM-score 1.00
- Q03386 · AlphaFold monomer V2.0 prediction for ral guanine nucleotide dissociation stimulator… · a predicted model of the same protein · chain A against A, TM-score 0.93
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 Q03386
- Every structure of UniProt P01112
- Elsewhere: RCSB PDB 1LFD · PDBe 1LFD · UniProt Q03386 · UniProt P01112
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