6V62: SETD3 double mutant

SETD3 double mutant (N255F/W273A) in Complex with an Actin Peptide with His73 Replaced with Lysine. Determined by X-ray diffraction at 2.36 Å resolution. Released 15 Jan 2020.

Method
X-ray diffraction
Resolution
2.36 Å
Organism
Homo sapiens
Chains
2
Atoms
4,213
Mol. weight
70.96 kDa
Ligands
SAH
Released
15 Jan 2020

Explore 6V62 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6V62 contains 28 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: 28 helices, 15 β-strands

ElementResiduesLengthSheet
α-helix21-3515
α-helix42-443
α-helix45-6016
α-helix74-774
α-helix78-869
β-strand95-10062
β-strand104-10962
β-strand11313
β-strand118-12361
α-helix124-1263
β-strand128-12924
α-helix130-1345
α-helix139-1446
α-helix146-1505
α-helix152-16413
α-helix172-1754
α-helix185-1873
α-helix190-1945
α-helix202-22524
α-helix227-2293
α-helix233-2353
α-helix240-25314
β-strand255-25844
β-strand265-26954
α-helix273-2753
β-strand277-27825
β-strand285-28841
β-strand293-29751
β-strand30213
β-strand307-30822
β-strand309-31025
α-helix317-3193
α-helix320-3245
β-strand335-34176
α-helix349-35810
β-strand364-37076
α-helix378-38710
α-helix391-3966
α-helix403-4086
α-helix419-43719
α-helix444-45310
α-helix458-49336
α-helix496-4994
Chain Y: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand7011

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Actin, cytoplasmic 1Yprotein23Homo sapiensP63261 (AlphaFold model)
Actin-histidine N-methyltransferaseAprotein596Homo sapiensQ86TU7 (AlphaFold model)
Sequence of entity 1 (Y), FASTA
>6V62_1 Actin, cytoplasmic 1 (chains Y)
TLKYPIEKGIVTNWDDMEKIWHH
Sequence of entity 2 (A), FASTA
>6V62_2 Actin-histidine N-methyltransferase (chains A)
GSMGKKSRVKTQKSGTGATATVSPKEILNLTSELLQKCSSPAPGPGKEWEEYVQIRTLVE
KIRKKQKGLSVTFDGKREDYFPDLMKWASENGASVEGFEMVNFKEEGFGLRATRDIKAEE
LFLWVPRKLLMTVESAKNSVLGPLYSQDRILQAMGNIALAFHLLCERASPNSFWQPYIQT
LPSEYDTPLYFEEDEVRYLQSTQAIHDVFSQYKNTARQYAYFYKVIQTHPHANKLPLKDS
FTYEDYRWAVSSVMTRQFQIPTEDGSRVTLALIPLADMCNHTNGLITTGYNLEDDRCECV
ALQDFRAGEQIYIFYGTRSNAEFVIHSGFFFDNNSHDRVKIKLGVSKSDRLYAMKAEVLA
RAGIPTSSVFALHFTEPPISAQLLAFLRVFCMTEEELKEHLLGDSAIDRIFTLGNSEFPV
SWDNEVKLWTFLEDRASLLLKTYKTTIEEDKSVLKNHDLSVRAKMAIKLRLGEKEILEKA
VKSAAVNREYYRQQMEEKAPLPKYEESNLGLLESSVGDSRLPLVLRNLEEEAGVQDALNI
REAISKAKATENGLVNGENSIPNGTRSENESLNQESKRAVEDAKGSSSDSTAGVKE

Ligands and cofactors

IDNameFormulaCopies
SAHS-adenosyl-L-homocysteineC14 H20 N6 O5 S1

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

Primary citation

An engineered variant of SETD3 methyltransferase alters target specificity from histidine to lysine methylation. Dai, S., Horton, J.R., Wilkinson, A.W. et al. J Biol Chem (2020) 295:2582-2589. DOI 10.1074/jbc.RA119.012319 · PubMed

Other PDB entries of the same protein (UniProt P63261 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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