6BCA: Transforming protein RhoA

A Complex between PH Domain of LbcRhoGEF (AKAP-Lbc) and Activated RhoA Bound to a GTP Analog. Determined by X-ray diffraction at 2.0 Å resolution. Released 13 Dec 2017.

Method
X-ray diffraction
Resolution
2.0 Å
Organism
Homo sapiens
Chains
4
Atoms
5,644
Mol. weight
77.84 kDa
Ligands
MG, GSP
Released
13 Dec 2017

Explore 6BCA in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6BCA contains 33 α-helices and 38 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: 5 helices, 13 β-strands

ElementResiduesLengthSheet
α-helix2194-220714
β-strand220812
β-strand2213-221533
α-helix22201
β-strand2221-222333
α-helix2224-22274
β-strand2232-2241102
β-strand2247-225592
β-strand2258-226582
β-strand2268-227142
α-helix2272-22732
β-strand227414
β-strand227714
β-strand2280-228232
β-strand2286-229052
β-strand2297-230262
β-strand2309-231462
α-helix2318-233215
Chain B: 6 helices, 13 β-strands
ElementResiduesLengthSheet
α-helix2197-220711
β-strand220815
β-strand2213-221536
α-helix22201
β-strand2221-222336
α-helix2224-22274
β-strand2232-2241105
α-helix22421
β-strand2247-225595
β-strand2258-226585
β-strand2268-227145
α-helix2272-22732
β-strand227417
β-strand227717
β-strand2280-228235
β-strand2286-229055
β-strand2297-230265
β-strand2309-231465
α-helix2318-233215
Chain C: 11 helices, 6 β-strands
ElementResiduesLengthSheet
β-strand4-1298
α-helix18-2710
β-strand39-48108
β-strand51-60108
α-helix64-663
α-helix70-734
β-strand79-8578
α-helix89-946
α-helix95-995
α-helix100-1067
β-strand112-11768
α-helix119-1213
α-helix125-1339
α-helix138-1403
α-helix141-15111
β-strand155-15848
α-helix167-17913
Chain F: 11 helices, 6 β-strands
ElementResiduesLengthSheet
β-strand4-1291
α-helix18-2710
β-strand39-48101
β-strand51-60101
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
α-helix167-17913

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Transforming protein RhoAC, Fprotein185Homo sapiensP61586 (AlphaFold model)
A-kinase anchor protein 13A, Bprotein151Homo sapiensQ12802 (AlphaFold model)
Sequence of entity 1 (C, F), FASTA
>6BCA_1 Transforming protein RhoA (chains C, F)
GILDMAAIRKKLVIVGDGACGKTCLLIVFSKDQFPEVYVPTVFENYVADIEVDGKQVELA
LWDTAGQEDYDRLRPLSYPDTDVILMCFSIDSPDSLENIPEKWTPEVKHFCPNVPIILVG
NKKDLRNDEHTRRELAKMKQEPVKPEEGRDMANRIGAFGYMECSAKTKDGVREVFEMATR
AALQA
Sequence of entity 2 (A, B), FASTA
>6BCA_2 A-kinase anchor protein 13 (chains A, B)
GILDASYEKKVRLNEIYTKTDSKSIMRMKSGQMFAKEDLKRKKLVRDGSVFLKNAAGRLK
EVQAVLLTDILVFLQEKDQKYIFASLDQKSTVISLKKLIVREVAHEEKGLFLISMGMTDP
EMVEVHASSKEERNSWIQIIQDTINHHHHHH

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg2
GSP5'-guanosine-diphosphate-monothiophosphateC10 H16 N5 O13 P3 S2

Primary citation

Crystal structures of the PH domains from Lbc family of RhoGEFs bound to activated RhoA GTPase. Chen, Z., Gutowski, S., Sternweis, P.C. Data Brief (2018) 17:356-362. DOI 10.1016/j.dib.2018.01.024 · PubMed

Other PDB entries of the same protein (UniProt P61586 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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