2JHT: Rhogdi K135T,K138T,K141T mutant

Crystal structure of rhogdi K135T,K138T,K141T mutant. Determined by X-ray diffraction at 1.88 Å resolution. Released 8 May 2007.

Method
X-ray diffraction
Resolution
1.88 Å
Organism
HOMO SAPIENS
Chains
4
Atoms
4,701
Mol. weight
63.05 kDa
Ligands
LI
Released
8 May 2007

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

Secondary structure: helices and β-sheets

2JHT contains 12 α-helices and 44 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: 3 helices, 11 β-strands

ElementResiduesLengthSheet
β-strand70-7891
β-strand87-8931
α-helix95-995
β-strand102-10542
β-strand109-11023
β-strand111-11881
β-strand123-134122
β-strand138-149122
β-strand152-15981
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-helix97-993
β-strand102-10545
β-strand109-11026
β-strand111-11884
β-strand123-133115
β-strand139-149115
α-helix1551
β-strand156-15944
α-helix160-1623
β-strand163-16426
β-strand173-182105
β-strand190-199105
Chain C: 3 helices, 11 β-strands
ElementResiduesLengthSheet
β-strand70-7897
β-strand87-8937
α-helix95-995
β-strand102-10548
β-strand109-11029
β-strand111-11887
β-strand123-134128
β-strand137-149138
α-helix1551
β-strand156-15947
α-helix160-1623
β-strand163-16429
β-strand173-182108
β-strand190-199108
Chain D: 3 helices, 11 β-strands
ElementResiduesLengthSheet
β-strand70-78910
β-strand87-89310
α-helix94-974
β-strand102-105411
β-strand109-110212
β-strand111-118810
β-strand123-1331111
β-strand138-1491211
α-helix1551
β-strand156-159410
α-helix160-1623
β-strand163-164212
β-strand173-1821011
β-strand188-1991211

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Rho GDP-dissociation inhibitor 1A, B, C, Dprotein138HOMO SAPIENSP52565 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>2JHT_1 RHO GDP-DISSOCIATION INHIBITOR 1 (chains A, B, C, D)
AMVPNVVVTGLTLVCSSAPGPLELDLTGDLESFKKQSFVLKEGVEYRIKISFRVNREIVS
GMKYIQHTYRTGVTIDTTDYMVGSYGPRAEEYEFLTPVEEAPKGMLARGSYSIKSRFTDD
DKTDHLSWEWNLTIKKDW

Ligands and cofactors

IDNameFormulaCopies
LILithium ionLi1

Water and common crystallization additives (SO4) are not listed.

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:

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