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Ec-NMR structure of human H-RAST35S mutant protein determined by combining evolutionary couplings (ec) and sparse NMR data
Analyse Ec-NMR structure of human H-RAST35S mutant protein determined by combining… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2N42
- Type
- protein
- Length
- 166 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P01112
Structure
solution nmr · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 166 | — | P01112 |
Compared structures
- 2N42 · EC-NMR Structure of Human H-RasT35S mutant protein Determined by Combining Evolutionary… · the same entry in another collection · chain A against A, TM-score 1.00
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 P01112
- Elsewhere: RCSB PDB 2N42 · PDBe 2N42 · UniProt P01112
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