4YON: P-Rex1:Rac1 complex

P-Rex1:Rac1 complex. Determined by X-ray diffraction at 1.95 Å resolution. Released 1 Jul 2015.

Method: X-ray diffraction
Resolution: 1.95 Å
Organism: Homo sapiens
Chains: 2
Atoms: 4,977
Mol. weight: 65.54 kDa
Released: 1 Jul 2015

Explore 4YON in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4YON contains 30 α-helices and 16 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: 19 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	36-71	36
α-helix	72-77	6
α-helix	78-81	4
α-helix	83-88	6
α-helix	93-100	8
α-helix	103-120	18
α-helix	132-138	7
α-helix	139-143	5
α-helix	144-162	19
α-helix	166-178	13
α-helix	186-187	2
α-helix	188-199	12
α-helix	202-211	10
α-helix	220-255	36
β-strand	257-258	2	1
α-helix	265-268	4
β-strand	272-281	10	1
β-strand	287-294	8	1
β-strand	297-303	7	1
α-helix	304	1
β-strand	325-332	8	1
α-helix	333-335	3
β-strand	336-340	5	1
β-strand	345	1	2
α-helix	353-354	2
β-strand	355	1	2
β-strand	358-363	6	1
β-strand	368-373	6	1
α-helix	377-397	21

Chain B: 11 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	3-10	8	3
α-helix	12-14	3
α-helix	16-24	9
β-strand	40-46	7	3
β-strand	49-56	8	3
α-helix	68-71	4
β-strand	77-83	7	3
α-helix	87-92	6
α-helix	93-97	5
α-helix	98-104	7
β-strand	110-115	6	3
α-helix	117-119	3
α-helix	123-130	8
α-helix	136-138	3
α-helix	139-149	11
β-strand	153-156	4	3
α-helix	165-174	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 1 protein	A	protein	405	Homo sapiens	Q8TCU6 (AlphaFold model)
Ras-related C3 botulinum toxin substrate 1	B	protein	179	Homo sapiens	P63000 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4YON_1 Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 1 protein (chains A)
GMEAPSGSEPGGDGAGDCAHPDPRAPGAAAPSSGPGPCAAARESERQLRLRLCVLNEILG
TERDYVGTLRFLQSAFLHRIRQNVADSVEKGLTEENVKVLFSNIEDILEVHKDFLAALEY
CLHPEPQSQHELGNVFLKFKDKFCVYEEYCSNHEKALRLLVELNKIPTVRAFLLSCMLLG
GRKTTDIPLEGYLLSPIQRICKYPLLLKELAKRTPGKHPDHPAVQSALQAMKTVCSNINE
TKRQMEKLEALEQLQSHIEGWEGSNLTDICTQLLLQGTLLKISAGNIQERAFFLFDNLLV
YCKRKSRVTGSKKSTKRTKSINGSLYIFRGRINTEVMEVENVEDGTADYHSNGYTVTNGW
KIHNTAKNKWFVCMAKTAEEKQKWLDAIIREREQRESLKLGMERD

Sequence of entity 2 (B), FASTA

>4YON_2 Ras-related C3 botulinum toxin substrate 1 (chains B)
GSMQAIKCVVVGDVAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPVNLGLWDT
AGQEDYDRLRPLSYPQTDVFLICFSLVSPASFENVRAKWYPEVRHHCPNTPIILVGTKLD
LRDDKDTIEKLKEKKLTPITYPQGLAMAKEIGAVKYLECSALTQRGLKTVFDEAIRAVL

Primary citation

The Phosphatidylinositol (3,4,5)-Trisphosphate-dependent Rac Exchanger 1Ras-related C3 Botulinum Toxin Substrate 1 (P-Rex1Rac1) Complex Reveals the Basis of Rac1 Activation in Breast Cancer Cells. Lucato, C.M., Halls, M.L., Ooms, L.M. et al. J Biol Chem (2015) 290:20827-20840. DOI 10.1074/jbc.M115.660456 · PubMed

Other PDB entries of the same protein (UniProt Q8TCU6 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5D3X 1.69 Å, Crystal Structure of the P-Rex1 PH domain with Inositol-(1,3,4,5)-Tetrakisphosphate Bound
5D3V 1.85 Å, Crystal Structure of the P-Rex1 PH domain with Citrate Bound
5D3W 1.85 Å, Crystal Structure of the P-Rex1 PH domain with Sulfate Bound
5D27 1.92 Å, Crystal Structure of the P-Rex1 PH domain
5D3Y 1.95 Å, Crystal Structure of the P-Rex1 PH domain with Inositol-(1,3,4,5)-Tetrakisphosphate Bound
3QIK 2.29 Å, Crystal structure of the first PDZ domain of PREX1
6VSK 3.12 Å, Crystal structure of the P-Rex1 DEP1 domain
6PCV 3.2 Å, Single Particle Reconstruction of Phosphatidylinositol (3,4,5) trisphosphate-dependent…
5FI1 3.2 Å, Crystal Structure of the P-Rex1 DH/PH tandem in complex with Cdc42
7RX9 3.22 Å, Structure of autoinhibited P-Rex1
5FI0 3.28 Å, Crystal Structure of the P-Rex1 DH/PH tandem in complex with Rac1
8TUA 4.1 Å, Full-length P-Rex1 in complex with inositol 1,3,4,5-tetrakisphosphate (IP4)

Browse structure collections

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