2VRW: Ras-related C3 botulinum toxin substrate 1

Critical structural role for the PH and C1 domains of the Vav1 exchange factor. Determined by X-ray diffraction at 1.85 Å resolution. Released 17 Jun 2008.

Method: X-ray diffraction
Resolution: 1.85 Å
Organisms: HOMO SAPIENS, MUS MUSCULUS
Chains: 2
Atoms: 4,883
Mol. weight: 68.09 kDa
Ligands: ZN
Released: 17 Jun 2008

Explore 2VRW in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2VRW contains 31 α-helices and 19 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: 10 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	3-10	8	1
α-helix	16-25	10
β-strand	40-46	7	1
β-strand	49-56	8	1
α-helix	68-71	4
β-strand	77-83	7	1
α-helix	87-92	6
α-helix	93-97	5
α-helix	98-104	7
β-strand	110-115	6	1
α-helix	117-120	4
α-helix	123-131	9
α-helix	136-138	3
α-helix	139-148	10
β-strand	153-156	4	1
α-helix	165-176	12

Chain B: 21 helices, 13 β-strands

Element	Residues	Length	Sheet
α-helix	191-215	25
α-helix	216-221	6
α-helix	222-224	3
α-helix	230-237	8
α-helix	240-259	20
α-helix	261-263	3
α-helix	266-273	8
α-helix	276-278	3
α-helix	279-300	22
α-helix	302-316	15
α-helix	322-325	4
α-helix	328-333	6
α-helix	336-346	11
α-helix	350-389	40
β-strand	390-391	2	2
α-helix	397-400	4
β-strand	403-412	10	2
β-strand	420-427	8	2
β-strand	430-437	8	2
β-strand	440-448	9	2
β-strand	452-455	4	2
β-strand	469-475	7	2
β-strand	481-486	6	2
α-helix	489-506	18
α-helix	513-515	3
β-strand	518-521	4	3
β-strand	528	1	4
α-helix	534	1
β-strand	535	1	4
α-helix	536	1
β-strand	543-546	4	3
β-strand	552-553	2	3
α-helix	555-560	6
α-helix	562-563	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ras-related C3 botulinum toxin substrate 1	A	protein	184	HOMO SAPIENS	P63000 (AlphaFold model)
Proto-oncogene vav	B	protein	406	MUS MUSCULUS	P27870 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2VRW_1 RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1 (chains A)
MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPVNLGLWDTAG
QEDYDRLRPLSYPQTDVFLICFSLVSPASFENVRAKWYPEVRHHCPNTPIILVGTKLDLR
DDKDTIEKLKEKKLTPITYPQGLAMAKEIGAVKYLECSALTQRGLKTVFDEAIRAVLCPP
PVKK

Sequence of entity 2 (B), FASTA

>2VRW_2 PROTO-ONCOGENE VAV (chains B)
GDEIYEDLMRLESVPTPPKMTEYDKRCCCLREIQQTEEKYTDTLGSIQQHFMKPLQRFLK
PQDMETIFVNIEELFSVHTHFLKELKDALAGPGATTLYQVFIKYKERFLVYGRYCSQVES
ASKHLDQVATAREDVQMKLEECSQRANNGRFTLRDLLMVPMQRVLKYHLLLQELVKHTQD
ATEKENLRLALDAMRDLAQCVNEVKRDNETLRQITNFQLSIENLDQSLANYGRPKIDGEL
KITSVERRSKTDRYAFLLDKALLICKRRGDSYDLKASVNLHSFQVRDDSSGERDNKKWSH
MFLLIEDQGAQGYELFFKTRELKKKWMEQFEMAISNIYPENATANGHDFQMFSFEETTSC
KACQMLLRGTFYQGYRCYRCRAPAHKECLGRVPPCGRHGQDFAGTM

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	2

Primary citation

Crucial Structural Role for the Ph and C1 Domains of the Vav1 Exchange Factor. Rapley, J., Tybulewicz, V., Rittinger, K. EMBO Rep (2008) 9:655. DOI 10.1038/EMBOR.2008.80 · PubMed

Other PDB entries of the same protein (UniProt P63000 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9RFF 1.25 Å, Crystal Structure of Human Rac1 Fused with the Scaffold Protein POSH (residues 319-371)
9IFK 1.34 Å, Crystal structure of Kalirin/Rac1 in complex with DK-2
1MH1 1.38 Å, Small G-protein
9HU8 1.48 Å, Crystal structure of Kalirin/Rac1 in complex with MC-278.
2WKQ 1.6 Å, Structure of a photoactivatable Rac1 containing the Lov2 C450A Mutant
6X1G 1.6 Å, Crystal structure of a GEF domain from the Orientia tsutsugamushi protein OtDUB in…
5O33 1.64 Å, A structure of the GEF Kalirin DH1 domain in complex with the small GTPase Rac1
9IG1 1.65 Å, Crystal structure of Kalirin/Rac1 in complex with DK-652
9I1L 1.68 Å, Crystal structure of Kalirin/Rac1 in complex with RS-009
8I5V 1.73 Å, DOCK10 mutant L1903Y complexed with Rac1
1RYF 1.75 Å, Alternative Splicing of Rac1 Generates Rac1b, a Self-activating GTPase
1RYH 1.75 Å, Alternative Splicing of Rac1 Generates Rac1b, a Self-activating GTPase

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