9CT8: Tricomplex of Compound 2, KRAS G12D, and CypA

Tricomplex of Compound 2, KRAS G12D, and CypA. Determined by X-ray diffraction at 1.28 Å resolution. Released 23 Jul 2025.

Method
X-ray diffraction
Resolution
1.28 Å
Organism
Homo sapiens
Chains
4
Atoms
6,362
Mol. weight
78.09 kDa
Ligands
GNP, MG, A1AZX
Released
23 Jul 2025

Explore 9CT8 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9CT8 contains 18 α-helices and 38 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 6 helices, 6 β-strands

ElementResiduesLengthSheet
β-strand2-1091
α-helix16-2510
β-strand37-46101
β-strand49-58101
α-helix65-7410
β-strand77-8371
α-helix87-915
α-helix93-10412
β-strand111-11661
α-helix127-13711
β-strand141-14331
α-helix152-16817
Chain B: 6 helices, 6 β-strands
ElementResiduesLengthSheet
β-strand1-10102
α-helix16-2510
β-strand37-46102
β-strand49-58102
α-helix65-7410
β-strand77-8372
α-helix87-915
α-helix93-10412
β-strand111-11662
α-helix127-13711
β-strand141-14332
α-helix152-16817
Chain C: 3 helices, 13 β-strands
ElementResiduesLengthSheet
β-strand5-1283
β-strand15-24103
α-helix30-4112
β-strand5213
β-strand55-5733
β-strand61-6443
β-strand7714
β-strand8014
β-strand8315
β-strand97-10043
β-strand10815
β-strand112-11543
α-helix120-1223
β-strand128-13253
α-helix136-1449
β-strand156-16493
Chain D: 3 helices, 13 β-strands
ElementResiduesLengthSheet
β-strand5-1286
β-strand15-24106
α-helix30-4112
β-strand5216
β-strand55-5736
β-strand61-6446
β-strand7717
β-strand8017
β-strand8318
β-strand97-10046
β-strand10818
β-strand112-11546
α-helix120-1223
β-strand128-13256
α-helix136-1438
β-strand156-16386

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Isoform 2B of GTPase KRasA, Bprotein170Homo sapiensP01116 (AlphaFold model)
Peptidyl-prolyl cis-trans isomerase AC, Dprotein166Homo sapiensP62937 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>9CT8_1 Isoform 2B of GTPase KRas (chains A, B)
SMTEYKLVVVGADGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTA
GQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCD
LPSRTVDTKQAQDLARSYGIPFIETSAKTRQGVDDAFYTLVREIRKHKEK
Sequence of entity 2 (C, D), FASTA
>9CT8_2 Peptidyl-prolyl cis-trans isomerase A (chains C, D)
SMVNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSCFHRIIPG
FMCQGGDFTRHNGTGGKSIYGEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKT
EWLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIADCGQLE

Ligands and cofactors

IDNameFormulaCopies
GNPPhosphoaminophosphonic acid-guanylate esterC10 H17 N6 O13 P32
MGMagnesium ionMg2
A1AZX(2R)-2-amino-N-(2-{[(1R)-1-cyclopentyl-2-{[(1M,8S,10S,14S,21M)-22-ethyl-4-hydro…C51 H68 N8 O82

Water and common crystallization additives (CL) are not listed.

Primary citation

A neomorphic protein interface catalyzes covalent inhibition of RAS G12D aspartic acid in tumors. Weller, C., Burnett, G.L., Jiang, L. et al. Science (2025) 389:eads0239-eads0239. DOI 10.1126/science.ads0239 · PubMed

Other PDB entries of the same protein (UniProt P01116 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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