3PCR: EspG-Arf6 complex

Structure of EspG-Arf6 complex. Determined by X-ray diffraction at 2.5 Å resolution. Released 5 Jan 2011.

Method: X-ray diffraction
Resolution: 2.5 Å
Organisms: Escherichia coli, Homo sapiens
Chains: 2
Atoms: 4,167
Mol. weight: 59.44 kDa
Ligands: MG, GTP
Released: 5 Jan 2011

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

Secondary structure: helices and β-sheets

3PCR contains 23 α-helices and 25 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: 16 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	50-60	11
α-helix	70-79	10
β-strand	83-85	3	1
α-helix	86-88	3
β-strand	91-98	8	1
β-strand	104-110	7	1
β-strand	114-120	7	1
β-strand	126-131	6	1
β-strand	146-147	2	2
β-strand	151	1	3
β-strand	153-156	4	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	220-222	3	2
α-helix	224-234	11
α-helix	242-244	3
α-helix	247-250	4
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	297-301	5
α-helix	304-315	12
β-strand	325-332	8	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: 7 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	15-20	6	4
α-helix	26-34	9
β-strand	41	1	3
β-strand	47-53	7	4
β-strand	58-64	7	4
α-helix	75-78	4
β-strand	83	1	5
β-strand	84-89	6	4
α-helix	96-108	13
α-helix	110-112	3
β-strand	116	1	5
β-strand	117-122	6	4
α-helix	129-131	3
α-helix	132-139	8
β-strand	149-154	6	4
α-helix	162-171	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
EspG	A	protein	357	Escherichia coli	Q7DB50 (AlphaFold model)
ADP-ribosylation factor 6	B	protein	162	Homo sapiens	P62330 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3PCR_1 EspG (chains A)
KKSWDEMSCAEKLFKVLSFGLWNPTYSRSERQSFQELLTVLEPVYPLPNELGRVSARFSD
GSSLRISVTNSELVEAEIRTANNEKITVLLESNEQNRLLQSLPIDRHMPYIQVHRALSEM
DLTDTTSMRNLLGFTSKLSTTLIPHNAQTDPLSGPTPFSSIFMDTCRGLGNAKLSLNGVD
IPANAQKLLRDALGLKDTHSSPTRNVIDHGISRHDAEQIARESSGSDKQKAEVVEFLCHP
EAATAICSAFYQSFNVPALTLTHERISKASEYNAERSLDTPNACINISISQSSDGNIYVT
SHTGVLIMAPEDRPNEMGMLTNRTSYEVPQGVKCIIDEMVSALQPRYAASETYLQNT

Sequence of entity 2 (B), FASTA

>3PCR_2 ADP-ribosylation factor 6 (chains B)
MRILMLGLDAAGKTTILYKLKLGQSVTTIPTVGFNVETVTYKNVKFNVWDVGGQDKIRPL
WRHYYTGTQGLIFVVDCADRDRIDEARQELHRIINDREMRDAIILIFANKQDLPDAMKPH
EIQEKLGLTRIRDRNWYVQPSCATSGDGLYEGLTWLTSNYKS

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	1
GTP	Guanosine-5'-triphosphate	C10 H16 N5 O14 P3	1

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:

4FMC 2.8 Å, EspG-Rab1 complex
3PCS 2.86 Å, Structure of EspG-PAK2 autoinhibitory Ialpha3 helix 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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