24SR: Human NRAS WT

Human NRAS WT (GDP-bound) in complex with macrocyclic peptide inhibitor AP6296. Determined by X-ray diffraction at 1.23 Å resolution. Released 16 Sept 2026.

Method: X-ray diffraction
Resolution: 1.23 Å
Organisms: Homo sapiens, synthetic construct
Chains: 6
Atoms: 5,033
Mol. weight: 66.56 kDa
Ligands: PO4, MG, GDP
Released: 16 Sept 2026

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

Secondary structure: helices and β-sheets

24SR contains 18 α-helices and 18 β-strands across 3 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: 5 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	2-10	9	1
α-helix	16-25	10
β-strand	38-46	9	1
β-strand	49-57	9	1
α-helix	66-74	9
β-strand	77-83	7	1
α-helix	87-104	18
β-strand	111-116	6	1
α-helix	127-137	11
β-strand	141-143	3	1
α-helix	152-168	17

Chain B: 6 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	2-10	9	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	152-168	17

Chain C: 7 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	2-10	9	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	87-91	5
α-helix	93-104	12
β-strand	111-116	6	3
α-helix	127-137	11
β-strand	141-143	3	3
α-helix	152-166	15
α-helix	167-169	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
GTPase NRas	A, B, C	protein	177	Homo sapiens	P01111 (AlphaFold model)
AP6296	I, J, K	protein	12	synthetic construct

Sequence of entity 1 (A, B, C), FASTA

>24SR_1 GTPase NRas (chains A, B, C)
GSSGGSTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDI
LDTAGQEEYSAMRDQYMRTGEGFLCVFAINNSKSFADINLYREQIKRVKDSDDVPMVLVG
NKCDLPTRTVDTKQAHELAKSYGIPFIETSAKTRQGVEDAFYTLVREIRQYRMKKLN

Sequence of entity 2 (I, J, K), FASTA

>24SR_2 AP6296 (chains I, J, K)
LIGGXGXPXAXX

Ligands and cofactors

ID	Name	Formula	Copies
PO4	Phosphate ion	O4 P	1
MG	Magnesium ion	Mg	3
GDP	Guanosine-5'-diphosphate	C10 H15 N5 O11 P2	3

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 P01111 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9BG8 1.2 Å, Tri-complex of Daraxonrasib (RMC-6236), NRAS Q61R, and CypA
7F68 1.24 Å, Crystal structure of N-ras S89D
9BG3 1.33 Å, Tri-complex of Daraxonrasib (RMC-6236), NRAS Q61K, and CypA
6ZIO 1.55 Å, Crystal structure of NRAS (C118S) in complex with GDP
9Y3W 1.56 Å, Crystal structure of NRas-G12D in complex with GDP and compound 13
8TBI 1.59 Å, Tricomplex of RMC-7977, NRAS WT, and CypA
9BG0 1.64 Å, Tri-complex of Daraxonrasib (RMC-6236), NRAS WT, and CypA
3CON 1.65 Å, Crystal structure of the human NRAS GTPase bound with GDP
6WGH 1.65 Å, Crystal structure of GDP-bound NRAS with ten residues long internal tandem duplication…
5UHV 1.67 Å, wild-type NRas bound to GppNHp
9Y1Y 1.7 Å, Crystal structure of NRas-G12D in complex with GDP and compound 7
9Y1X 1.72 Å, Crystal structure of NRas-G12D in complex with GDP and IACS-56676

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