MolNFT v1 · #45096 · protein
NMR data-driven model of GTPase KRAS-GNP:ARAFRBD complex tethered to a lipid-bilayer nanodisc
2MSE: “NMR data-driven model of GTPase KRAS-GNP:ARAFRBD complex tethered to a lipid-bilayer nanodisc”. Solution nmr. MolNFT v1 #45096 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2MSE
- Type
- protein
- Length
- 654 residues
- Chains
- 4
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P02647, P01116, P10398
Structure
solution nmr · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | — | protein | 198 | — | P02647 |
| B | — | protein | 185 | — | P01116 |
| D | — | protein | 73 | — | P10398 |
Compared structures
- 2MSE · NMR data-driven model of GTPase KRas-GNP:ARafRBD complex tethered to a lipid-bilayer… · the same entry in another collection · chain A against A, TM-score 1.00
- P10398 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase a-RAF (P10398) · a predicted model of the same protein · chain D against A, TM-score 0.93
- P02647 · AlphaFold monomer V2.0 prediction for apolipoprotein a-I (P02647) · a predicted model of the same protein · chain A against A, TM-score 0.58
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 P02647
- Every structure of UniProt P01116
- Every structure of UniProt P10398
- Elsewhere: RCSB PDB 2MSE · PDBe 2MSE · UniProt P02647 · UniProt P01116 · UniProt P10398
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