3P71: Complex of LCMT-1 and PP2A

Crystal structure of the complex of LCMT-1 and PP2A. Determined by X-ray diffraction at 2.7 Å resolution. Released 16 Feb 2011.

Method
X-ray diffraction
Resolution
2.7 Å
Organism
Homo sapiens
Chains
2
Atoms
5,159
Mol. weight
74.15 kDa
Ligands
AN6, MN
Released
16 Feb 2011

Explore 3P71 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3P71 contains 32 α-helices and 24 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 C: 15 helices, 15 β-strands

ElementResiduesLengthSheet
α-helix3-1816
α-helix21-244
α-helix25-3915
β-strand45-4842
α-helix491
β-strand52-5543
α-helix62-7211
β-strand80-8233
α-helix93-10614
β-strand111-11333
α-helix121-1244
α-helix129-1368
α-helix141-15010
β-strand156-15942
β-strand163-16642
α-helix178-1814
α-helix188-1903
α-helix194-2007
β-strand202-20324
β-strand21115
β-strand21815
β-strand219-22024
α-helix222-23211
β-strand236-23942
β-strand248-25142
β-strand256-25942
α-helix265-2673
β-strand273-27863
β-strand284-28963
α-helix302-3065
Chain T: 17 helices, 9 β-strands
ElementResiduesLengthSheet
α-helix23-4220
α-helix51-533
α-helix61-633
α-helix64-8825
β-strand93-9751
α-helix104-1107
β-strand117-12261
α-helix124-13613
α-helix138-1469
β-strand15411
β-strand159-16131
β-strand165-16951
α-helix175-18410
β-strand193-19861
α-helix201-2033
α-helix206-21914
β-strand223-23081
α-helix236-24712
α-helix255-2573
α-helix261-27010
β-strand275-28061
α-helix281-2866
α-helix290-2978
α-helix305-3128
β-strand315-32281
α-helix329-3313

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Leucine carboxyl methyltransferase 1Tprotein334Homo sapiensQ9UIC8 (AlphaFold model)
Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoformCprotein304Homo sapiensP67775 (AlphaFold model)
Sequence of entity 1 (T), FASTA
>3P71_1 Leucine carboxyl methyltransferase 1 (chains T)
MATRQRESSITSCCSTSSMDENDEGVRGTCEDASLCKRFAVSIGYWHDPYIQHFVRLSKE
RKAPEINRGYFARVHGVSQLIKAFLRKTECHCQIVNLGAGMDTTFWRLKDEDLLSSKYFE
VDFPMIVTRKLHSIKCKPPLSSPILELHSEDTLQMDGHILDSKRYAVIGADLRDLSELEE
KLKKCNMNTQLPTLLIAECVLVYMTPEQSANLLKWAANSFERAMFINYEQVNMGDRFGQI
MIENLRRRQCDLAGVETCKSLESQKERLLSNGWETASAVDMMELYNRLPRAEVSRIESLE
FLDEMELLEQLMRHYCLCWATKGGNELGLKEITY
Sequence of entity 2 (C), FASTA
>3P71_2 Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform (chains C)
MDEKVFTKELDQWIEQLNECKQLSESQVKSLCEKAKEILTKESNVQEVRCPVTVCGDVHG
QFHDLMELFRIGGKSPDTNYLFMGDYVDRGYYSVETVTLLVALKVRYRERITILRGNHES
RQITQVYGFYDECLRKYGNANVWKYFTDLFDYLPLTALVDGQIFCLHGGLSPSIDTLDHI
RALDRLQEVPHEGPMCDLLWSDPDDRGGWGISPRGAGYTFGQDISETFNHANGLTLVSRA
HQLVMEGYNWCHDRNVVTIFSAPNYCYRCGNQAAIMELDDTLKYSFLQFDPAPHVTRRTP
DYFL

Ligands and cofactors

IDNameFormulaCopies
AN65'-{[(3S)-3-amino-3-carboxypropyl](ethyl)amino}-5'-deoxyadenosineC16 H25 N7 O51
MNManganese (II) ionMn2

Water and common crystallization additives (PEG) are not listed.

Primary citation

The Structural Basis for Tight Control of PP2A Methylation and Function by LCMT-1. Stanevich, V., Jiang, L., Satyshur, K.A. et al. Mol Cell (2011) 41:331-342. DOI 10.1016/j.molcel.2010.12.030 · PubMed

Other PDB entries of the same protein (UniProt Q9UIC8 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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