7VV9: HRas(GMPPNP-bound)

Crystal Structure of HRas(GMPPNP-bound) in complex with the Ras-binding domain(RBD) of SIN1. Determined by X-ray diffraction at 1.6 Å resolution. Released 18 May 2022.

Method: X-ray diffraction
Resolution: 1.6 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,307
Mol. weight: 29.66 kDa
Ligands: MG, GNP
Released: 18 May 2022

Explore 7VV9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7VV9 contains 9 α-helices and 12 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: 7 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	3-10	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	87-91	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	152-164	13

Chain C: 2 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	279-285	7	1
β-strand	288-294	7	1
β-strand	300	1	2
α-helix	301-313	13
β-strand	323-327	5	1
β-strand	340	1	2
α-helix	341-344	4
β-strand	348-353	6	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
GTPase HRas	A	protein	170	Homo sapiens	P01112 (AlphaFold model)
Target of rapamycin complex 2 subunit MAPKAP1	C	protein	86	Homo sapiens	Q9BPZ7 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>7VV9_1 GTPase HRas (chains A)
MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAG
QEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDL
AARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQHKLRK

Sequence of entity 2 (C), FASTA

>7VV9_2 Target of rapamycin complex 2 subunit MAPKAP1 (chains C)
SKESLFVRINAAHGFSLIQVDNTKVTMKEILLKAVKRRKGSQKVSGPQYRLEKQSEPNVA
VDLDSTLESQSAWEFCLVRENSSRAD

Ligands and cofactors

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

Primary citation

Structural insights into Ras regulation by SIN1. Zheng, Y., Ding, L., Meng, X. et al. Proc Natl Acad Sci U S A (2022) 119:e2119990119-e2119990119. DOI 10.1073/pnas.2119990119 · 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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