MolNFT v1 · #157532 · protein

Tetrahydropyridopyrimidines as covalent inhibitors of KRAS-G12C

6N2J · GTPase KRAS: “Tetrahydropyridopyrimidines as covalent inhibitors of KRAS-G12C”. X-ray diffraction, 3 ligands (GDP, K9M, MG), 1 pocket (best druggability 0.71). MolNFT v1 #157532 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 6N2J
Type: protein
Length: 168 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: GTPase KRAS
UniProt: P01116
Ligands: GDP, K9M, MG
Pockets: 1 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	GTPase KRAS	protein	168	38% helix, 24% strand	P01116

Ligands and binding sites

GDP · Guanosine-5'-diphosphate · ligand · chains A
K9M · 1-{4-[7-(naphthalen-1-yl)-5,6,7,8-tetrahydropyrido[3,4-d]pyrimidin-4-yl]piperazin-1-yl}propan-1-one · ligand · chains A
MG · Magnesium ion · metal · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	305	0.71	0.84	43	GDP, MG, K9M

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

6N2J · Tetrahydropyridopyrimidines as Covalent Inhibitors of KRAS-G12C · 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 P01116
Elsewhere: RCSB PDB 6N2J · PDBe 6N2J · UniProt P01116

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