MolNFT v1 · #145662 · protein

RAS:SOS:RAS in complex with a small molecule activator

6CUP: “RAS:SOS:RAS in complex with a small molecule activator”. X-ray diffraction, 4 ligands (GNP, FFV, MG). MolNFT v1 #145662 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6CUP
Type: protein
Length: 802 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P01112, Q07889
Ligands: GNP, FFV, MG, NA

Structure

x-ray diffraction · 3 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	166	—	P01112
B	—	protein	469	—	Q07889
C	—	protein	167	—	P01112

Ligands and binding sites

GNP · Phosphoaminophosphonic acid-guanylate ester · ligand · chains A
FFV · N~2~-(3-chloro-4-fluorophenyl)-N~4~-[(1R)-1-cyclopropylethyl]quinazoline-2,4-diamine · ligand · chains B
MG · Magnesium ion · metal · chains A
NA · Sodium ion · metal · chains C
FMT · Formic acid · additive · 6 copies · chains B, A, C
GOL · Glycerol · additive · 2 copies · chains B

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

Compared structures

6CUP · Ras:SOS:Ras in complex with a small molecule activator · the same entry in another collection · chain A against A, TM-score 1.00
Q07889 · AlphaFold monomer V2.0 prediction for son of sevenless homolog 1 (Q07889) · a predicted model of the same protein · chain B 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 P01112
Every structure of UniProt Q07889
Elsewhere: RCSB PDB 6CUP · PDBe 6CUP · UniProt P01112 · UniProt Q07889

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