5M70: Human RhoGAP mutated in its arginin finger

Crystal Structure of human RhoGAP mutated in its arginin finger (R85A) in complex with RhoA.GDP.AlF4- human. Determined by X-ray diffraction at 2.2 Å resolution. Released 17 May 2017.

Method
X-ray diffraction
Resolution
2.2 Å
Organism
Homo sapiens
Chains
4
Atoms
5,933
Mol. weight
98.79 kDa
Ligands
ALF, GDP, MG
Released
17 May 2017

Explore 5M70 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5M70 contains 55 α-helices and 14 β-strands across 4 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: 17 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix49-557
α-helix64-7613
α-helix90-10112
α-helix104-1063
α-helix108-1103
α-helix115-12612
α-helix135-1373
α-helix138-1425
α-helix144-1463
α-helix149-1513
α-helix152-1609
α-helix165-18319
α-helix185-1884
α-helix192-20312
α-helix209-2146
α-helix216-22813
α-helix230-2334
Chain B: 11 helices, 8 β-strands
ElementResiduesLengthSheet
β-strand6-1271
α-helix18-269
β-strand39-4681
β-strand53-6081
α-helix64-663
α-helix70-734
β-strand79-8571
α-helix89-946
α-helix95-995
α-helix100-1067
β-strand112-11761
α-helix119-1213
α-helix125-1328
α-helix138-1403
α-helix141-15111
β-strand155-15841
β-strand16012
β-strand16512
α-helix167-17812
Chain F: 16 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix49-557
α-helix64-7613
α-helix90-10213
α-helix104-1063
α-helix108-1103
α-helix115-12612
α-helix135-1373
α-helix138-1425
α-helix144-1463
α-helix152-16110
α-helix165-18319
α-helix185-1884
α-helix192-20312
α-helix209-2146
α-helix216-22813
α-helix230-2334
Chain G: 11 helices, 6 β-strands
ElementResiduesLengthSheet
β-strand6-1271
α-helix18-2710
β-strand39-4681
β-strand53-6081
α-helix64-663
α-helix70-734
β-strand79-8571
α-helix89-946
α-helix95-995
α-helix100-1067
β-strand112-11761
α-helix119-1224
α-helix125-1328
α-helix138-1403
α-helix141-15111
β-strand155-15841
α-helix167-17812

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Rho GTPase-activating protein 1A, Fprotein240Homo sapiensQ07960 (AlphaFold model)
Transforming protein RhoAB, Gprotein192Homo sapiensP61586 (AlphaFold model)
Sequence of entity 1 (A, F), FASTA
>5M70_1 Rho GTPase-activating protein 1 (chains A, F)
HVKLEQLGIPRQVLKYDDFLKSTQKSPATAPKPMPPRPPLPNQQFGVSLQHLQEKNPEQE
PIPIVLRETVAYLQAHALTTEGIFARSANTQVVREVQQKYNMGLPVDFDQYNELHLPAVI
LKTFLRELPEPLLTFDLYPHVVGFLNIDESQRVPATLQVLQTLPEENYQVLRFLTAFLVQ
ISAHSDQNKMTNTNLAVVFGPNLLWAKDAAITLKAINPINTFTKFLLDHQGELFPSPDPS
Sequence of entity 2 (B, G), FASTA
>5M70_2 Transforming protein RhoA (chains B, G)
AAIRKKLVIVGDGACGKTCLLIVNSKDQFPEVYVPTVFENYVADIEVDGKQVELALWDTA
GQEDYDRLRPLSYPDTDVILMCFSIDSPDSLENIPEKWTPEVKHFCPNVPIILVGNKKDL
RNDEHTRRELAKMKQEPVKPEEGRDMANRIGAFGYMECSAKTKDGVREVFEMATRAALQA
RRGKKKSGCLVL

Ligands and cofactors

IDNameFormulaCopies
ALFTetrafluoroaluminate ionAl F42
GDPGuanosine-5'-diphosphateC10 H15 N5 O11 P22
MGMagnesium ionMg2

Primary citation

Assessing the Influence of Mutation on GTPase Transition States by Using X-ray Crystallography, (19) F NMR, and DFT Approaches. Jin, Y., Molt, R.W., Pellegrini, E. et al. Angew Chem Int Ed Engl (2017) 56:9732-9735. DOI 10.1002/anie.201703074 · PubMed

Other PDB entries of the same protein (UniProt Q07960 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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