2V1Y: PDB entry 2V1Y

Structure of a phosphoinositide 3-kinase alpha adaptor-binding domain (ABD) in a complex with the iSH2 domain from p85 alpha. Determined by X-ray diffraction at 2.4 Å resolution. Released 24 Jul 2007.

Method: X-ray diffraction
Resolution: 2.4 Å
Organisms: BOS TAURUS, HOMO SAPIENS
Chains: 2
Atoms: 2,234
Mol. weight: 34.04 kDa
Released: 24 Jul 2007

Explore 2V1Y in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2V1Y contains 9 α-helices and 9 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: 5 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	19-25	7	1
β-strand	31-37	7	1
β-strand	41	1	2
α-helix	42-52	11
α-helix	53-55	3
α-helix	59-61	3
α-helix	65-67	3
β-strand	69-73	5	1
β-strand	74	1	3
β-strand	79-82	4	1
β-strand	88	1	2
α-helix	89-91	3
β-strand	94	1	3
β-strand	98-102	5	1

Chain B: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	434-435	2
α-helix	439-512	74
α-helix	518-586	69
α-helix	591-598	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit alpha isoform	A	protein	108	BOS TAURUS	P32871 (AlphaFold model)
Phosphatidylinositol 3-kinase regulatory subunit alpha	B	protein	170	HOMO SAPIENS	P27986 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2V1Y_1 PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE 3-KINASE CATALYTIC SUBUNIT ALPHA ISOFORM (chains A)
MPPRPSSGELWGIHLMPPRILVECLLPNGMIVTLECLREATLITIKHELFKEARKYPLHQ
LLQDESSYIFVSVTQEAEREEFFDETRRLCDLRLFQPFLKVIEPVGNR

Sequence of entity 2 (B), FASTA

>2V1Y_2 PHOSPHATIDYLINOSITOL 3-KINASE REGULATORY SUBUNIT ALPHA (chains B)
YQQDQVVKEDNIEAVGKKLHKYNTQFQEKSREYDRLYEEYTRTSQEIQMKRTAIEAFNET
IKIFEEQCQTQERYSKEYIEKFKREGNEKEIQRIMHNYDKLKSRISEIIDSRRRLEEDLK
KQAAEYREIDKRMNSIKPDLIQLRKTRDQYLMWLTQKGVRQKKLNEWLGN

Primary citation

Mechanism of Two Classes of Cancer Mutations in the Phosphoinositide 3-Kinase Catalytic Subunit. Miled, N., Yan, Y., Hon, W.C. et al. Science (2007) 317:239. DOI 10.1126/SCIENCE.1135394 · PubMed

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