4IYP: NPP2Ac-alpha4 complex

structure of the nPP2Ac-alpha4 complex. Determined by X-ray diffraction at 2.8 Å resolution. Released 17 Apr 2013.

Method: X-ray diffraction
Resolution: 2.8 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,708
Mol. weight: 43.82 kDa
Released: 17 Apr 2013

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

Secondary structure: helices and β-sheets

4IYP contains 18 α-helices and 3 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: 11 helices, 0 β-strands

Element	Residues	Length
α-helix	2-5	4
α-helix	12-27	16
α-helix	36-59	24
α-helix	68-70	3
α-helix	76-80	5
α-helix	81-90	10
α-helix	95-97	3
α-helix	98-118	21
α-helix	125-142	4
α-helix	156-180	25
α-helix	186-219	34

Chain C: 7 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	9-18	10
α-helix	21-24	4
α-helix	25-39	15
β-strand	61-63	3	1
β-strand	79-83	5	1
α-helix	94-107	14
α-helix	108-110	3
β-strand	111-114	4	1
α-helix	127-136	10
α-helix	141-150	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Immunoglobulin-binding protein 1	A	protein	222	Homo sapiens	P78318 (AlphaFold model)
Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform	C	protein	151	Homo sapiens	P67775 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4IYP_1 Immunoglobulin-binding protein 1 (chains A)
GSMAAEDELQLPRLPELFETGRQLLDEVEVATEPAGSRIVQEKVFKGLDLLEKAAEMLSQ
LDLFSRNEDLEEIASTDLKYLLVPAFQGALTMKQVNPSKRLDHLQRAREHFINYLTQCHC
YHVAEFELPSMAYPSLVAMASQRQAKIQRYKQKKELEHRLSAMKSAVESGQADDERVREY
YLLHLQRWIDISLEEIESIDQEIKILRERDSSREASTSNSSR

Sequence of entity 2 (C), FASTA

>4IYP_2 Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform (chains C)
GSMFTKELDQWIEQLNECKQLSESQVKSLCEKAKEILTKESNVQEVRCPVTVCGDVHGQF
HDLMELFRIGGKSPDTNYLFMGDYVDRGYYSVETVTLLVALKVRYRERITILRGNHESRQ
ITQVYGFYDECLRKYGNANVWKYFTDLFDYL

Primary citation

Structural basis of protein phosphatase 2A stable latency. Jiang, L., Stanevich, V., Satyshur, K.A. et al. Nat Commun (2013) 4:1699-1699. DOI 10.1038/ncomms2663 · PubMed

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