6O07: PDB entry 6O07

Structure and mechanism of acetylation by the N-terminal dual enzyme NatA/Naa50 complex. Determined by X-ray diffraction at 2.7 Å resolution. Released 12 Jun 2019.

Method
X-ray diffraction
Resolution
2.7 Å
Organism
Saccharomyces cerevisiae
Chains
3
Atoms
9,036
Mol. weight
149.95 kDa
Ligands
ACO, MLI, IHP
Released
12 Jun 2019

Explore 6O07 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6O07 contains 64 α-helices and 17 β-strands across 3 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: 50 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix55-6713
α-helix70-8314
α-helix91-10313
α-helix107-11913
α-helix127-13711
α-helix141-15414
α-helix159-17113
α-helix175-18814
α-helix198-21619
α-helix220-23314
α-helix234-2363
α-helix240-25314
α-helix257-27014
α-helix275-28511
α-helix287-2893
α-helix291-30414
α-helix310-3134
α-helix314-3174
α-helix322-33918
α-helix344-35411
α-helix356-37217
α-helix380-39617
α-helix400-41314
α-helix418-43114
α-helix434-44714
α-helix452-46413
α-helix468-4758
α-helix488-4936
α-helix497-52226
α-helix535-55824
α-helix560-57011
α-helix575-5828
α-helix585-59511
α-helix598-6003
α-helix602-62221
α-helix659-6657
α-helix683-6864
α-helix691-6955
α-helix696-7005
α-helix701-7066
α-helix709-7113
α-helix714-7229
α-helix727-74014
α-helix746-75813
α-helix767-78115
α-helix787-7904
α-helix797-8059
α-helix810-8189
α-helix827-83610
α-helix843-8519
Chain B: 9 helices, 9 β-strands
ElementResiduesLengthSheet
β-strand3-753
α-helix10-123
α-helix13-219
α-helix30-378
β-strand45-4953
β-strand85-8734
β-strand90-9124
β-strand92-10093
β-strand112-12093
α-helix122-1243
α-helix129-14517
β-strand149-15243
α-helix159-1624
α-helix163-1686
β-strand172-17323
β-strand190-19343
α-helix196-1994
α-helix201-2033
Chain C: 5 helices, 8 β-strands
ElementResiduesLengthSheet
β-strand7-931
α-helix16-2510
β-strand61-6661
β-strand69-7681
β-strand93-9861
α-helix100-1023
α-helix107-12014
β-strand126-13272
α-helix137-1404
α-helix142-1443
β-strand148-14922
β-strand15412
β-strand168-17472

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
N-terminal acetyltransferase A complex subunit NAT5Cprotein176Saccharomyces cerevisiaeQ08689 (AlphaFold model)
Naa15Aprotein854Saccharomyces cerevisiaeP12945 (AlphaFold model)
N-terminal acetyltransferase A complex catalytic subunit ARD1Bprotein238Saccharomyces cerevisiaeP07347 (AlphaFold model)
Sequence of entity 1 (C), FASTA
>6O07_1 N-terminal acetyltransferase A complex subunit NAT5 (chains C)
MGRDICTLDNVYANNLGMLTKLAHVTVPNLYQDAFFSALFAEDSLVAKNKKPSSKKDVHF
TQMAYYSEIPVGGLVAKLVPKKQNELSLKGIQIEFLGVLPNYRHKSIGSKLLKFAEDKCS
ECHQHNVFVYLPAVDDLTKQWFIAHGFEQVGETVNNFIKGVNGDEQDAILLKKHIS
Sequence of entity 2 (A), FASTA
>6O07_2 Naa15 (chains A)
MSRKRSTKPKPAAKIALKKENDQFLEALKLYEGKQYKKSLKLLDAILKKDGSHVDSLALK
GLDLYSVGEKDDAASYVANAIRKIEGASASPICCHVLGIYMRNTKEYKESIKWFTAALNN
GSTNKQIYRDLATLQSQIGDFKSALVSRKKYWEAFLGYRANWTSLAVAQDVNGERQQAIN
TLSQFEKLAEGKISDSEKYEHSECLMYKNDVMYKAASDNQDKLQNVLKHLNDIEPCVFDK
FGLLERKATIYMKLGQLKDASIVYRTLIKRNPDNFKYYKLLEVSLGIQGDNKLKKALYGK
LEQFYPRCEPPKFIPLTFLQDKEELSKKLREYVLPQLKRGVPATFSNVKPLYQRRKSKVS
PLLEKIVLDYLSGLDPTQDPIPFIWTNYYLSQHFLFLKDFPKAQEYIDAALDHTPTLVEF
YILKARILKHLGLMDTAAGILEEGRQLDLQDRFINCKTVKYFLRANNIDKAVEVASLFTK
NDDSVNGIKDLHLVEASWFIVEQAEAYYRLYLDRKKKLDDLESLKKEVESDKSEQIANDI
KENQWLVRKYKGLALKRFNAIPKFYKQFEDDQLDFHSYCMRKGTPRAYLEMLEWGKALYT
KPMYVRAMKEASKLYFQMHDDRLKRKSDSLDENSDEIQNNGQNSSSQKKKAKKEAAAMNK
RKETEAKSVAAYPSDQDNDVFGEKLIETSTPMEDFATEFYNNYSMQVREDERDYILDFEF
NYRIGKLALCFASLNKFAKRFGTTSGLFGSMAIVLLHATRNDTPFDPILKKVVTKSLEKE
YSENFPLNEISNNSFDWLNFYQEKFGKNDINGLLFLYRYRDDVPIGSSNLKEMIISSLSP
LEPHSQNEILQYYL
Sequence of entity 3 (B), FASTA
>6O07_3 N-terminal acetyltransferase A complex catalytic subunit ARD1 (chains B)
MPINIRRATINDIICMQNANLHNLPENYMMKYYMYHILSWPEASFVATTTTLDCEDSDEQ
DENDKLELTLDGTNDGRTIKLDPTYLAPGEKLVGYVLVKMNDDPDQQNEPPNGHITSLSV
MRTYRRMGIAENLMRQALFALREVHQAEYVSLHVRQSNRAALHLYRDTLAFEVLSIEKSY
YQDGEDAYAMKKVLKLEELQISNFTHRRLKENEEKLEDDLESDLLEDIIKQGVNDIIV

Ligands and cofactors

IDNameFormulaCopies
ACOAcetyl coenzyme *aC23 H38 N7 O17 P3 S1
MLIMalonate ionC3 H2 O44
IHPInositol hexakisphosphateC6 H18 O24 P61

Water and common crystallization additives (CL, GOL, EPE) are not listed.

Primary citation

Structure and Mechanism of Acetylation by the N-Terminal Dual Enzyme NatA/Naa50 Complex. Deng, S., Magin, R.S., Wei, X. et al. Structure (2019) 27:1057. DOI 10.1016/j.str.2019.04.014 · PubMed

Other PDB entries of the same protein (UniProt Q08689 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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