8VM2: NRAS Q61K

Crystal Structure of NRAS Q61K bound to GTP. Determined by X-ray diffraction at 1.74 Å resolution. Released 1 May 2024.

Method: X-ray diffraction
Resolution: 1.74 Å
Organism: Homo sapiens
Chains: 3
Atoms: 4,818
Mol. weight: 68.04 kDa
Ligands: GTP, MG
Released: 1 May 2024

Explore 8VM2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8VM2 contains 21 α-helices and 20 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: 7 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	-3--2	2	1
β-strand	1-9	9	1
α-helix	16-25	10
β-strand	37-46	10	1
β-strand	49-58	10	1
α-helix	62-67	6
α-helix	68-74	7
β-strand	77-83	7	1
α-helix	87-91	5
α-helix	93-104	12
β-strand	111-116	6	1
α-helix	127-137	11
β-strand	141-143	3	1
α-helix	152-169	18

Chain B: 7 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	-3--2	2	2
β-strand	1-9	9	2
α-helix	16-25	10
β-strand	37-46	10	2
β-strand	49-58	10	2
α-helix	62-67	6
α-helix	68-74	7
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	152-170	19

Chain C: 7 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	2-10	9	3
α-helix	16-25	10
β-strand	37-46	10	3
β-strand	49-58	10	3
α-helix	62-64	3
α-helix	68-74	7
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	152-169	18

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
GTPase NRas	A, B, C	protein	190	Homo sapiens	P01111 (AlphaFold model)

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

>8VM2_1 GTPase NRas (chains A, B, C)
MHHHHHHSSGRENLYFQGMTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRK
QVVIDGETCLLDILDTAGKEEYSAMRDQYMRTGEGFLCVFAINNSKSFADINLYREQIKR
VKDSDDVPMVLVGNKCDLPTRTVDTKQAHELAKSYGIPFIETSAKTRQGVEDAFYTLVRE
IRQYRMKKLN

Ligands and cofactors

ID	Name	Formula	Copies
GTP	Guanosine-5'-triphosphate	C10 H16 N5 O14 P3	5
MG	Magnesium ion	Mg	3

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

Primary citation

Crystal structure of NRAS Q61K with a ligand-induced pocket near switch II. Gebregiworgis, T., Chan, J.Y., Kuntz, D.A. et al. Eur J Cell Biol (2024) 103:151414-151414. DOI 10.1016/j.ejcb.2024.151414 · PubMed

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
24SR 1.23 Å, Human NRAS WT (GDP-bound) in complex with macrocyclic peptide inhibitor AP6296
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

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