24SQ: Human HRAS WT

Human HRAS WT (GDP-bound) in complex with macrocyclic peptide inhibitor AP6296. Determined by X-ray diffraction at 1.08 Å resolution. Released 16 Sept 2026.

Method: X-ray diffraction
Resolution: 1.08 Å
Organisms: Homo sapiens, synthetic construct
Chains: 4
Atoms: 3,495
Mol. weight: 43.06 kDa
Ligands: GDP, MG
Released: 16 Sept 2026

Explore 24SQ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

24SQ contains 11 α-helices and 14 β-strands across 2 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, 8 β-strands

Element	Residues	Length	Sheet
β-strand	-3--2	2	1
β-strand	1-2	2	1
β-strand	3-10	8	2
α-helix	16-25	10
β-strand	38-46	9	2
β-strand	49-57	9	2
α-helix	66-74	9
β-strand	77-83	7	2
α-helix	87-91	5
α-helix	93-104	12
β-strand	111-116	6	2
α-helix	127-137	11
β-strand	141-143	3	2
α-helix	152-164	13

Chain B: 5 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	2-9	8	3
α-helix	16-25	10
β-strand	38-46	9	3
β-strand	49-57	9	3
α-helix	66-74	9
β-strand	77-83	7	3
α-helix	87-104	18
β-strand	111-116	6	3
α-helix	127-137	11
β-strand	141-143	3	3
α-helix	152-164	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
GTPase HRas, N-terminally processed	A, B	protein	171	Homo sapiens	P01112 (AlphaFold model)
AP6296	I, J	protein	12	synthetic construct

Sequence of entity 1 (A, B), FASTA

>24SQ_1 GTPase HRas, N-terminally processed (chains A, B)
GSSGGSTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDI
LDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQYREQIKRVKDSDDVPMVLVG
NKCDLAARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQH

Sequence of entity 2 (I, J), FASTA

>24SQ_2 AP6296 (chains I, J)
LIGGXGXPXAXX

Ligands and cofactors

ID	Name	Formula	Copies
GDP	Guanosine-5'-diphosphate	C10 H15 N5 O11 P2	2
MG	Magnesium ion	Mg	2

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

Primary citation

Exploiting Bridged Conformations for Precise Molecular Recognition in the Design of KRAS-Selective, Orally Available Macrocyclic Peptides. Kage, M., Kawada, H., Takano, K. et al. J Am Chem Soc (2026). DOI 10.1021/jacs.6c14212

Other PDB entries of the same protein (UniProt P01112 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2CE2 1.0 Å, Crystal structure analysis of a fluorescent form of H-ras P21 in complex with GDP
2EVW 1.05 Å, Crystal structure analysis of a fluorescent form of H-Ras p21 in complex with R-caged GTP
8TBG 1.2 Å, Tricomplex of RMC-7977, HRAS WT, and CypA
2CLD 1.22 Å, Crystal structure analysis of a fluorescent form of H-ras P21 in complex with GDP (2)
2CL6 1.24 Å, Crystal structure analysis of a fluorescent form of H-ras P21 in complex with S-caged GTP
2CL7 1.25 Å, Crystal structure analysis of a fluorescent form of H-ras P21 in complex with GTP
5WDQ 1.25 Å, H-Ras mutant L120A bound to GMP-PNP at 100K
1CTQ 1.26 Å, Structure of P21RAS in complex with gppnhp at 100 K
2CLC 1.3 Å, Crystal structure analysis of a fluorescent form of H-ras P21 in complex with GTP (2)
3K8Y 1.3 Å, Allosteric modulation of H-Ras GTPase
3OIW 1.3 Å, H-RasG12V with allosteric switch in the "on" state
3TGP 1.31 Å, Room temperature H-ras

Browse structure collections

About this viewer

MolViewer shows 24SQ directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.