4HNX: The NatA Acetyltransferase Complex

Name: PDB 4HNX: The NatA Acetyltransferase Complex Bound To ppGpp
Published: 2014-03-26
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: transferase

The NatA Acetyltransferase Complex Bound To ppGpp. Determined by X-ray diffraction at 2.34 Å resolution. Released 26 Mar 2014.

Method: X-ray diffraction
Resolution: 2.34 Å
Organism: Saccharomyces cerevisiae S288c
Chains: 2
Atoms: 7,408
Mol. weight: 129.56 kDa
Ligands: G4P
Released: 26 Mar 2014

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

Secondary structure: helices and β-sheets

4HNX contains 61 α-helices and 9 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: 47 helices, 0 β-strands

Element	Residues	Length
α-helix	19-32	14
α-helix	36-48	13
α-helix	54-66	13
α-helix	70-82	13
α-helix	91-103	13
α-helix	107-119	13
α-helix	126-137	12
α-helix	141-154	14
α-helix	159-171	13
α-helix	175-189	15
α-helix	195-197	3
α-helix	198-216	19
α-helix	220-233	14
α-helix	234-236	3
α-helix	240-253	14
α-helix	257-270	14
α-helix	275-285	11
α-helix	291-304	14
α-helix	309-313	5
α-helix	314-317	4
α-helix	322-338	17
α-helix	344-354	11
α-helix	356-372	17
α-helix	380-396	17
α-helix	400-413	14
α-helix	418-430	13
α-helix	434-446	13
α-helix	452-464	13
α-helix	468-475	8
α-helix	476-478	3
α-helix	497-519	23
α-helix	535-570	36
α-helix	575-582	8
α-helix	585-595	11
α-helix	598-600	3
α-helix	602-621	20
α-helix	683-686	4
α-helix	691-695	5
α-helix	696-700	5
α-helix	701-706	6
α-helix	709-711	3
α-helix	714-722	9
α-helix	727-741	15
α-helix	746-756	11
α-helix	810-817	8
α-helix	828-836	9
α-helix	843-852	10

Chain B: 14 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	1
α-helix	10-12	3
α-helix	13-18	6
α-helix	26-39	14
β-strand	45-49	5	1
β-strand	85-87	3	2
β-strand	90-91	2	2
β-strand	92-100	9	1
α-helix	104-106	3
α-helix	110-111	2
β-strand	112-120	9	1
α-helix	122-124	3
α-helix	129-145	17
β-strand	149-155	7	1
α-helix	159-162	4
α-helix	163-168	6
β-strand	172-177	6	1
β-strand	187-193	7	1
α-helix	196-199	4
α-helix	201-204	4
α-helix	226-229	4
α-helix	233-238	6
α-helix	240-242	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
N-terminal acetyltransferase A complex subunit NAT1	A	protein	863	Saccharomyces cerevisiae S288c	P12945 (AlphaFold model)
N-terminal acetyltransferase A complex catalytic subunit ARD1	B	protein	248	Saccharomyces cerevisiae S288c	P07347 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4HNX_1 N-terminal acetyltransferase A complex subunit NAT1 (chains A)
MSRKRSTKPKPAAKIALKKENDQFLEALKLYEGKQYKKSLKLLDAILKKDGSHVDSLALK
GLDLYSVGEKDDAASYVANAIRKIEGASASPICCHVLGIYMRNTKEYKESIKWFTAALNN
GSTNKQIYRDLATLQSQIGDFKNALVSRKKYWEAFLGYRANWTSLAVAQDVNGERQQAIN
TLSQFEKLAEGKISDSEKYEHSECLMYKNDIMYKAASDNQDKLQNVLKHLNDIEPCVFDK
FGLLERKATIYMKLGQLKDASIVYRTLIKRNPDNFKYYKLLEVSLGIQGDNKLKKALYGK
LEQFYPRCEPPKFIPLTFLQDKEELSKKLREYVLPQLERGVPATFSNVKPLYQRRKSKVS
PLLEKIVLDYLSGLDPTQDPIPFIWTNYYLSQHFLFLKDFPKAQEYIDAALDHTPTLVEF
YILKARILKHLGLMDTAAGILEEGRQLDLQDRFINCKTVKYFLRANNIDKAVEVASLFTK
NDDSVNGIKDLHLVEASWFIVEQAEAYYRLYLDRKKKLDDLASLKKEVESDKSEQIANDI
KENQWLVRKYKGLALKRFNAIPKFYKQFEDDQLDFHSYCMRKGTPRAYLEMLEWGKALYT
KPMYVRAMKEASKLYFQMHDDRLKRKSDSLDENSDEIQNNGQNSSSQKKKAKKEAAAMNK
RKETEAKSVAAYPSDQDNDVFGEKLIETSTPMEDFATEFYNNYSMQVREDERDYILDFEF
NYRIGKLALCFASLNKFAKRFGTTSGLFGSMAIVLLHATRNDTPFDPILKKVVTKSLEKE
YSENFPLNEISNNSFDWLNFYQEKFGKNDINGLLFLYRYRDDVPIGSSNLKEMIISSLSP
LEPHSQNEILQYYLYPYDVPDYA

Sequence of entity 2 (B), FASTA

>4HNX_2 N-terminal acetyltransferase A complex catalytic subunit ARD1 (chains B)
MPINIRRATINDIICMQNANLHNLPENYMMKYYMYHILSWPEASFVATTTTLDCEDSDEQ
DENDKLELTLDGTNDGRTIKLDPTYLAPGEKLVGYVLVKMNDDPDQQNEPPNGHITSLSV
MRTYRRMGIAENLMRQALFALREVHQAEYVSLHVRQSNRAALHLYRDTLAFEVLSIEKSY
YQDGEDAYAMKKVLKLEELQISNFTHRRLKENEEKLEDDLESDLLEDIIKQGVNDIIVEQ
KLISEEDL

Ligands and cofactors

ID	Name	Formula	Copies
G4P	Guanosine-5',3'-tetraphosphate	C10 H17 N5 O17 P4	1

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.

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…
4HNY 2.25 Å, Apo N-terminal acetyltransferase complex A
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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