NMR data-driven model of GTPase KRAS-GNP:ARAFRBD complex tethered to a lipid-bilayer nanodisc

Structure

solution nmr · 3 distinct chains · 60% helix, 17% strand (DSSP).

Ligands and binding sites

• PCW · 1,2-dioleoyl-sn-glycero-3-phosphocholine · ligand · 64 copies · chains A, C, B, D
• 17F · O-[(S)-({(2R)-2,3-bis[(9Z)-octadec-9-enoyloxy]propyl}oxy)(hydroxy)phosphoryl]-L-serine · ligand · 16 copies · chains D, C
• GNP · Phosphoaminophosphonic acid-guanylate ester · ligand · chains B
• MG · Magnesium ion · metal · chains B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Interfaces

3 interfaces between chains.

• A–C · 3977 Ų buried · 68 hydrogen bonds · protein-protein
• B–D · 600 Ų buried · 17 hydrogen bonds · protein-protein
• A–B · 203 Ų buried · 4 hydrogen bonds · protein-protein

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