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
| Element | Residues | Length | Sheet |
|---|
| α-helix | 50-60 | 11 | |
| α-helix | 70-79 | 10 | |
| β-strand | 82-85 | 4 | 1 |
| β-strand | 91-98 | 8 | 1 |
| β-strand | 104-110 | 7 | 1 |
| β-strand | 115-120 | 6 | 1 |
| β-strand | 126-131 | 6 | 1 |
| α-helix | 135-137 | 3 | |
| α-helix | 139-142 | 4 | |
| β-strand | 146-147 | 2 | 2 |
| β-strand | 154-156 | 3 | 2 |
| α-helix | 166-176 | 11 | |
| β-strand | 181-183 | 3 | 2 |
| α-helix | 202-209 | 8 | |
| β-strand | 214-217 | 4 | 2 |
| β-strand | 220-221 | 2 | 2 |
| α-helix | 224-234 | 11 | |
| α-helix | 245-250 | 6 | |
| α-helix | 254-262 | 9 | |
| β-strand | 265 | 1 | 2 |
| α-helix | 268-278 | 11 | |
| α-helix | 281-290 | 10 | |
| α-helix | 293-296 | 4 | |
| α-helix | 297-315 | 19 | |
| β-strand | 324-332 | 9 | 2 |
| β-strand | 338-349 | 12 | 2 |
| α-helix | 350-351 | 2 | |
| β-strand | 358-369 | 12 | 2 |
| α-helix | 377-383 | 7 | |
| β-strand | 387-394 | 8 | 2 |
Chain B: 16 helices, 17 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 50-60 | 11 | |
| α-helix | 70-79 | 10 | |
| β-strand | 82-84 | 3 | 3 |
| β-strand | 91-98 | 8 | 3 |
| β-strand | 104-110 | 7 | 3 |
| β-strand | 115-120 | 6 | 3 |
| β-strand | 126-131 | 6 | 3 |
| α-helix | 139-142 | 4 | |
| β-strand | 146-147 | 2 | 4 |
| β-strand | 151 | 1 | 5 |
| β-strand | 153-156 | 4 | 4 |
| α-helix | 166-176 | 11 | |
| β-strand | 181-184 | 4 | 4 |
| β-strand | 186 | 1 | 6 |
| α-helix | 202-209 | 8 | |
| β-strand | 214-217 | 4 | 4 |
| β-strand | 220-222 | 3 | 4 |
| α-helix | 224-234 | 11 | |
| α-helix | 241-244 | 4 | |
| α-helix | 245-250 | 6 | |
| α-helix | 254-262 | 9 | |
| β-strand | 265 | 1 | 4 |
| α-helix | 268-278 | 11 | |
| α-helix | 281-289 | 9 | |
| α-helix | 293-296 | 4 | |
| α-helix | 297-312 | 16 | |
| α-helix | 315-317 | 3 | |
| β-strand | 324-332 | 9 | 4 |
| β-strand | 338-349 | 12 | 4 |
| α-helix | 350-351 | 2 | |
| β-strand | 358-369 | 12 | 4 |
| α-helix | 377-383 | 7 | |
| β-strand | 387-394 | 8 | 4 |
Chain C: 15 helices, 17 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 50-61 | 12 | |
| α-helix | 70-79 | 10 | |
| β-strand | 82-84 | 3 | 7 |
| β-strand | 91-98 | 8 | 7 |
| β-strand | 104-110 | 7 | 7 |
| β-strand | 115-120 | 6 | 7 |
| β-strand | 126-131 | 6 | 7 |
| β-strand | 146-147 | 2 | 8 |
| β-strand | 151 | 1 | 6 |
| β-strand | 153-156 | 4 | 8 |
| α-helix | 166-176 | 11 | |
| β-strand | 181-184 | 4 | 8 |
| β-strand | 186 | 1 | 5 |
| α-helix | 202-207 | 6 | |
| β-strand | 214-217 | 4 | 8 |
| β-strand | 220-222 | 3 | 8 |
| α-helix | 224-234 | 11 | |
| α-helix | 242-244 | 3 | |
| α-helix | 245-250 | 6 | |
| α-helix | 254-262 | 9 | |
| β-strand | 265 | 1 | 8 |
| α-helix | 268-278 | 11 | |
| α-helix | 281-290 | 10 | |
| α-helix | 294-296 | 3 | |
| α-helix | 297-308 | 12 | |
| α-helix | 310-313 | 4 | |
| β-strand | 324-332 | 9 | 8 |
| β-strand | 338-349 | 12 | 8 |
| α-helix | 350-351 | 2 | |
| β-strand | 358-369 | 12 | 8 |
| α-helix | 377-383 | 7 | |
| β-strand | 387-394 | 8 | 8 |
Chain D: 12 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 50-58 | 9 | |
| α-helix | 71-79 | 9 | |
| β-strand | 83-84 | 2 | 9 |
| β-strand | 91-98 | 8 | 9 |
| β-strand | 104-110 | 7 | 9 |
| β-strand | 115-120 | 6 | 9 |
| β-strand | 126-131 | 6 | 9 |
| β-strand | 146-147 | 2 | 10 |
| β-strand | 154-156 | 3 | 10 |
| α-helix | 166-176 | 11 | |
| β-strand | 181-184 | 4 | 10 |
| α-helix | 202-207 | 6 | |
| β-strand | 214-217 | 4 | 10 |
| β-strand | 220-222 | 3 | 10 |
| α-helix | 224-234 | 11 | |
| α-helix | 245-250 | 6 | |
| α-helix | 254-262 | 9 | |
| β-strand | 265 | 1 | 10 |
| α-helix | 268-278 | 11 | |
| α-helix | 281-291 | 11 | |
| α-helix | 294-296 | 3 | |
| α-helix | 297-315 | 19 | |
| β-strand | 324-330 | 7 | 10 |
| β-strand | 338-349 | 12 | 10 |
| β-strand | 358-369 | 12 | 10 |
| α-helix | 377-381 | 5 | |
| β-strand | 387-394 | 8 | 10 |
Chains E and H: 1 helix, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 123-126 | 4 | |
| β-strand | 129 | 1 | 2 |
Chains F and G: 1 helix, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 124-126 | 3 | |
| β-strand | 129 | 1 | 4 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| EspG | A, B, C, D | protein | 357 | Escherichia coli | Q7DB50 (AlphaFold model) |
| Serine/threonine-protein kinase PAK 2 | E, F, G, H | protein | 16 | Homo sapiens | Q13177 (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:
- 3PCR 2.5 Å, Structure of EspG-Arf6 complex
- 4FMC 2.8 Å, EspG-Rab1 complex
- 4FMD 3.05 Å, EspG-Rab1 complex structure at 3.05 A
- 4FME 4.1 Å, EspG-Rab1-Arf6 complex
Browse structure collections
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