2JHX: Rhogdi E155H, E157H mutant

Crystal structure of rhogdi E155H, E157H mutant. Determined by X-ray diffraction at 1.6 Å resolution. Released 8 May 2007.

Method
X-ray diffraction
Resolution
1.6 Å
Organism
HOMO SAPIENS
Chains
2
Atoms
2,652
Mol. weight
31.63 kDa
Released
8 May 2007

Explore 2JHX in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2JHX contains 7 α-helices and 22 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: 4 helices, 11 β-strands

ElementResiduesLengthSheet
β-strand70-7891
β-strand87-8931
α-helix94-996
β-strand102-10542
β-strand109-11023
β-strand111-11881
β-strand123-134122
β-strand137-149132
α-helix1551
β-strand156-15941
α-helix160-1623
β-strand163-16423
α-helix169-1713
β-strand173-182102
β-strand190-199102
Chain B: 3 helices, 11 β-strands
ElementResiduesLengthSheet
β-strand70-7894
β-strand87-8934
α-helix94-996
β-strand102-10545
β-strand109-11026
β-strand111-11884
β-strand123-134125
β-strand137-149135
α-helix1551
β-strand156-15944
α-helix160-1623
β-strand163-16426
β-strand173-182105
β-strand190-199105

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Rho GDP-dissociation inhibitor 1A, Bprotein138HOMO SAPIENSP52565 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>2JHX_1 RHO GDP-DISSOCIATION INHIBITOR 1 (chains A, B)
AMVPNVVVTGLTLVCSSAPGPLELDLTGDLESFKKQSFVLKEGVEYRIKISFRVNREIVS
GMKYIQHTYRKGVKIDKTDYMVGSYGPRAEHYHFLTPVEEAPKGMLARGSYSIKSRFTDD
DKTDHLSWEWNLTIKKDW

Primary citation

Protein Crystallization by Surface Entropy Reduction: Optimization of the Ser Strategy. Cooper, D.R., Boczek, T., Grelewska, K. et al. Acta Crystallogr D Biol Crystallogr (2007) 63:636. DOI 10.1107/S0907444907010931 · PubMed

Other PDB entries of the same protein (UniProt P52565 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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