1HH4: Ras-related C3 botulinum toxin substrate 1

Rac1-RhoGDI complex involved in NADPH oxidase activation. Determined by X-ray diffraction at 2.7 Å resolution. Released 28 Aug 2001.

Method
X-ray diffraction
Resolution
2.7 Å
Organism
HOMO SAPIENS
Chains
4
Atoms
5,908
Mol. weight
90.73 kDa
Ligands
GER, MG, GDP
Released
28 Aug 2001

Explore 1HH4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1HH4 contains 35 α-helices and 37 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: 13 helices, 9 β-strands

ElementResiduesLengthSheet
β-strand211
β-strand5-1061
α-helix16-249
α-helix37-393
β-strand40-4561
β-strand50-5781
α-helix62-643
α-helix68-714
β-strand77-8371
α-helix87-926
α-helix93-975
α-helix98-1047
β-strand110-11561
α-helix117-1193
α-helix125-1284
α-helix136-1383
α-helix139-14911
β-strand153-15641
β-strand15812
β-strand16312
α-helix165-17612
α-helix180-1823
Chain B: 11 helices, 8 β-strands
ElementResiduesLengthSheet
β-strand2-1093
α-helix16-249
β-strand42-4543
β-strand50-5783
α-helix68-714
β-strand77-8373
α-helix87-926
α-helix93-975
α-helix98-1047
β-strand110-11563
α-helix117-1193
α-helix125-1284
α-helix130-1323
α-helix136-1383
α-helix139-14911
β-strand153-15643
β-strand15814
β-strand16314
α-helix165-17612
Chain D: 5 helices, 10 β-strands
ElementResiduesLengthSheet
α-helix328-3314
α-helix335-3395
α-helix346-35611
β-strand370-379105
β-strand387-38935
α-helix395-3984
β-strand401-40446
β-strand409-418105
β-strand423-433116
β-strand438-449126
β-strand456-45945
α-helix460-4623
β-strand463-46425
β-strand474-48296
β-strand490-49896
Chain E: 6 helices, 10 β-strands
ElementResiduesLengthSheet
α-helix329-3313
α-helix335-3395
α-helix346-35611
β-strand370-379107
β-strand386-38947
α-helix395-3984
β-strand401-40558
β-strand409-418107
β-strand423-433118
β-strand438-449128
β-strand456-45947
α-helix460-4623
β-strand463-46427
α-helix468-4714
β-strand474-48298
β-strand490-499108

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Ras-related C3 botulinum toxin substrate 1A, Bprotein192HOMO SAPIENSP63000 (AlphaFold model)
Rho GDP-dissociation inhibitor 1D, Eprotein204HOMO SAPIENSP52565 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>1HH4_1 RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1 (chains A, B)
PQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPVNLGLWDTAG
QEDYDRLRPLSYPQTDVSLICFSLVSPASFENVRAKWYPEVRHHCPNTPIILVGTKLDLR
DDKDTIEKLKEKKLTPITYPQGLAMAKEIGAVKYLECSALTQRGLKTVFDEAIRAVLCPP
PVKKRKRKCLLL
Sequence of entity 2 (D, E), FASTA
>1HH4_2 RHO GDP-DISSOCIATION INHIBITOR 1 (chains D, E)
MAEQEPTAEQLAQIAAENEEDEHSVNYKPPAQKSIQEIQELDKDDESLRKYKEALLGRVA
VSADPNVPNVVVTGLTLVCSSAPGPLELDLTGDLESFKKQSFVLKEGVEYRIKISFRVNR
EIVSGMKYIQHTYRKGVKIDKTDYMVGSYGPRAEEYEFLTPVEEAPKGMLARGSYSIKSR
FTDDDKTDHLSWEWNLTIKKDWKD

Ligands and cofactors

IDNameFormulaCopies
GERGeran-8-yl geranC20 H342
MGMagnesium ionMg2
GDPGuanosine-5'-diphosphateC10 H15 N5 O11 P22

Primary citation

Crystal Structure of the Rac1-Rhogdi Complex Involved in Nadph Oxidase Activation. Grizot, S., Faure, J., Fieschi, F. et al. Biochemistry (2001) 40:10007. DOI 10.1021/BI010288K · PubMed

Other PDB entries of the same protein (UniProt P63000 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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