4HNY: Apo N-terminal acetyltransferase complex A

Apo N-terminal acetyltransferase complex A. Determined by X-ray diffraction at 2.25 Å resolution. Released 26 Mar 2014.

Method

X-ray diffraction

Resolution

2.25 Å

Organism

Saccharomyces cerevisiae S288c

Chains

4

Atoms

16,053

Mol. weight

259.36 kDa

Released

26 Mar 2014

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

Secondary structure: helices and β-sheets

4HNY contains 120 α-helices and 18 β-strands across 4 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: 46 helices, 4 β-strands

Molecules and chains

>4HNY_1 N-terminal acetyltransferase A complex subunit NAT1 (chains A, C)
MSRKRSTKPKPAAKIALKKENDQFLEALKLYEGKQYKKSLKLLDAILKKDGSHVDSLALK
GLDLYSVGEKDDAASYVANAIRKIEGASASPICCHVLGIYMRNTKEYKESIKWFTAALNN
GSTNKQIYRDLATLQSQIGDFKNALVSRKKYWEAFLGYRANWTSLAVAQDVNGERQQAIN
TLSQFEKLAEGKISDSEKYEHSECLMYKNDIMYKAASDNQDKLQNVLKHLNDIEPCVFDK
FGLLERKATIYMKLGQLKDASIVYRTLIKRNPDNFKYYKLLEVSLGIQGDNKLKKALYGK
LEQFYPRCEPPKFIPLTFLQDKEELSKKLREYVLPQLERGVPATFSNVKPLYQRRKSKVS
PLLEKIVLDYLSGLDPTQDPIPFIWTNYYLSQHFLFLKDFPKAQEYIDAALDHTPTLVEF
YILKARILKHLGLMDTAAGILEEGRQLDLQDRFINCKTVKYFLRANNIDKAVEVASLFTK
NDDSVNGIKDLHLVEASWFIVEQAEAYYRLYLDRKKKLDDLASLKKEVESDKSEQIANDI
KENQWLVRKYKGLALKRFNAIPKFYKQFEDDQLDFHSYCMRKGTPRAYLEMLEWGKALYT
KPMYVRAMKEASKLYFQMHDDRLKRKSDSLDENSDEIQNNGQNSSSQKKKAKKEAAAMNK
RKETEAKSVAAYPSDQDNDVFGEKLIETSTPMEDFATEFYNNYSMQVREDERDYILDFEF
NYRIGKLALCFASLNKFAKRFGTTSGLFGSMAIVLLHATRNDTPFDPILKKVVTKSLEKE
YSENFPLNEISNNSFDWLNFYQEKFGKNDINGLLFLYRYRDDVPIGSSNLKEMIISSLSP
LEPHSQNEILQYYLYPYDVPDYA

>4HNY_2 N-terminal acetyltransferase A complex catalytic subunit ARD1 (chains B, D)
MPINIRRATINDIICMQNANLHNLPENYMMKYYMYHILSWPEASFVATTTTLDCEDSDEQ
DENDKLELTLDGTNDGRTIKLDPTYLAPGEKLVGYVLVKMNDDPDQQNEPPNGHITSLSV
MRTYRRMGIAENLMRQALFALREVHQAEYVSLHVRQSNRAALHLYRDTLAFEVLSIEKSY
YQDGEDAYAMKKVLKLEELQISNFTHRRLKENEEKLEDDLESDLLEDIIKQGVNDIIVEQ
KLISEEDL

Primary citation

The Protein Complex NatA Binds Inositol Hexakisphosphate and Exhibits Conformational Flexibility. Neubauer, J.L., Pham, T., Immormino, R.M. et al. To be published.

Related structures

Other PDB entries of the same protein (UniProt P12945 (AlphaFold model), which also has an AlphaFold model), best resolution first:

• 4XNH 2.1 Å, Crystal structure of yeast N-terminal acetyltransferase NatE (IP6) in complex with a…
• 4HNX 2.34 Å, The NatA Acetyltransferase Complex Bound To ppGpp
• 6O07 2.7 Å, Structure and mechanism of acetylation by the N-terminal dual enzyme NatA/Naa50 complex
• 4HNW 2.8 Å, The NatA Acetyltransferase Complex Bound To Inositol Hexakisphosphate
• 4XPD 2.81 Å, Crystal structure of yeast N-terminal acetyltransferase NatE (ppGpp) in complex with a…
• 6HD7 3.4 Å, Cryo-EM structure of the ribosome-NatA complex
• 4Y49 3.95 Å, Crystal structure of yeast N-terminal acetyltransferase (ppGpp) NatE in complex with a…
• 6HD5 4.8 Å, Cryo-EM structure of the ribosome-NatA complex

Browse structure collections

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