3OIU: GTPase HRas

H-RasQ61L with allosteric switch in the "on" state. Determined by X-ray diffraction at 1.32 Å resolution. Released 8 Dec 2010.

Method: X-ray diffraction
Resolution: 1.32 Å
Organism: Homo sapiens
Chains: 1
Atoms: 1,548
Mol. weight: 19.61 kDa
Ligands: MG, CA, GNP
Released: 8 Dec 2010

Explore 3OIU in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3OIU contains 6 α-helices and 6 β-strands across 1 chain. 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

Element	Residues	Length	Sheet
β-strand	2-9	8	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	87-104	18
β-strand	111-116	6	1
α-helix	127-137	11
β-strand	141-143	3	1
α-helix	152-163	12

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
GTPase HRas	A	protein	166	Homo sapiens	P01112 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3OIU_1 GTPase HRas (chains A)
MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAG
LEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDL
AARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQH

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	2
CA	Calcium ion	Ca	3
GNP	Phosphoaminophosphonic acid-guanylate ester	C10 H17 N6 O13 P3	1

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

Primary citation

Allosteric Modulation of Ras-GTP Is Linked to Signal Transduction through RAF Kinase. Buhrman, G., Kumar, V.S., Cirit, M. et al. J Biol Chem (2011) 286:3323-3331. DOI 10.1074/jbc.M110.193854 · PubMed

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
24SQ 1.08 Å, Human HRAS WT (GDP-bound) in complex with macrocyclic peptide inhibitor AP6296
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

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