3PCS: EspG-PAK2 autoinhibitory Ialpha3 helix complex

Structure of EspG-PAK2 autoinhibitory Ialpha3 helix complex. Determined by X-ray diffraction at 2.86 Å resolution. Released 5 Jan 2011.

Method
X-ray diffraction
Resolution
2.86 Å
Organisms
Escherichia coli, Homo sapiens
Chains
8
Atoms
11,254
Mol. weight
165.81 kDa
Released
5 Jan 2011

Explore 3PCS in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3PCS contains 62 α-helices and 68 β-strands across 8 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: 15 helices, 15 β-strands

ElementResiduesLengthSheet
α-helix50-6011
α-helix70-7910
β-strand82-8541
β-strand91-9881
β-strand104-11071
β-strand115-12061
β-strand126-13161
α-helix135-1373
α-helix139-1424
β-strand146-14722
β-strand154-15632
α-helix166-17611
β-strand181-18332
α-helix202-2098
β-strand214-21742
β-strand220-22122
α-helix224-23411
α-helix245-2506
α-helix254-2629
β-strand26512
α-helix268-27811
α-helix281-29010
α-helix293-2964
α-helix297-31519
β-strand324-33292
β-strand338-349122
α-helix350-3512
β-strand358-369122
α-helix377-3837
β-strand387-39482
Chain B: 16 helices, 17 β-strands
ElementResiduesLengthSheet
α-helix50-6011
α-helix70-7910
β-strand82-8433
β-strand91-9883
β-strand104-11073
β-strand115-12063
β-strand126-13163
α-helix139-1424
β-strand146-14724
β-strand15115
β-strand153-15644
α-helix166-17611
β-strand181-18444
β-strand18616
α-helix202-2098
β-strand214-21744
β-strand220-22234
α-helix224-23411
α-helix241-2444
α-helix245-2506
α-helix254-2629
β-strand26514
α-helix268-27811
α-helix281-2899
α-helix293-2964
α-helix297-31216
α-helix315-3173
β-strand324-33294
β-strand338-349124
α-helix350-3512
β-strand358-369124
α-helix377-3837
β-strand387-39484
Chain C: 15 helices, 17 β-strands
ElementResiduesLengthSheet
α-helix50-6112
α-helix70-7910
β-strand82-8437
β-strand91-9887
β-strand104-11077
β-strand115-12067
β-strand126-13167
β-strand146-14728
β-strand15116
β-strand153-15648
α-helix166-17611
β-strand181-18448
β-strand18615
α-helix202-2076
β-strand214-21748
β-strand220-22238
α-helix224-23411
α-helix242-2443
α-helix245-2506
α-helix254-2629
β-strand26518
α-helix268-27811
α-helix281-29010
α-helix294-2963
α-helix297-30812
α-helix310-3134
β-strand324-33298
β-strand338-349128
α-helix350-3512
β-strand358-369128
α-helix377-3837
β-strand387-39488
Chain D: 12 helices, 15 β-strands
ElementResiduesLengthSheet
α-helix50-589
α-helix71-799
β-strand83-8429
β-strand91-9889
β-strand104-11079
β-strand115-12069
β-strand126-13169
β-strand146-147210
β-strand154-156310
α-helix166-17611
β-strand181-184410
α-helix202-2076
β-strand214-217410
β-strand220-222310
α-helix224-23411
α-helix245-2506
α-helix254-2629
β-strand265110
α-helix268-27811
α-helix281-29111
α-helix294-2963
α-helix297-31519
β-strand324-330710
β-strand338-3491210
β-strand358-3691210
α-helix377-3815
β-strand387-394810
Chains E and H: 1 helix, 1 β-strand
ElementResiduesLengthSheet
α-helix123-1264
β-strand12912
Chains F and G: 1 helix, 1 β-strand
ElementResiduesLengthSheet
α-helix124-1263
β-strand12914

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
EspGA, B, C, Dprotein357Escherichia coliQ7DB50 (AlphaFold model)
Serine/threonine-protein kinase PAK 2E, F, G, Hprotein16Homo sapiensQ13177 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>3PCS_1 EspG (chains A, B, C, D)
KKSWDEMSCAEKLFKVLSFGLWNPTYSRSERQSFQELLTVLEPVYPLPNELGRVSARFSD
GSSLRISVTNSELVEAEIRTANNEKITVLLESNEQNRLLQSLPIDRHMPYIQVHRALSEM
DLTDTTSMRNLLGFTSKLSTTLIPHNAQTDPLSGPTPFSSIFMDTCRGLGNAKLSLNGVD
IPANAQKLLRDALGLKDTHSSPTRNVIDHGISRHDAEQIARESSGSDKQKAEVVEFLCHP
EAATAICSAFYQSFNVPALTLTHERISKASEYNAERSLDTPNACINISISQSSDGNIYVT
SHTGVLIMAPEDRPNEMGMLTNRTSYEVPQGVKCIIDEMVSALQPRYAASETYLQNT
Sequence of entity 2 (E, F, G, H), FASTA
>3PCS_2 Serine/threonine-protein kinase PAK 2 (chains E, F, G, H)
QAVLDVLKFYDSNTVK

Primary citation

The assembly of a GTPase-kinase signalling complex by a bacterial catalytic scaffold. Selyunin, A.S., Sutton, S.E., Weigele, B.A. et al. Nature (2011) 469:107-111. DOI 10.1038/nature09593 · PubMed

Other PDB entries of the same protein (UniProt Q7DB50 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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