4HNW: The NatA Acetyltransferase Complex

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

The NatA Acetyltransferase Complex Bound To Inositol Hexakisphosphate. Determined by X-ray diffraction at 2.8 Å resolution. Released 26 Mar 2014.

Method: X-ray diffraction
Resolution: 2.8 Å
Organism: Saccharomyces cerevisiae S288c
Chains: 2
Atoms: 7,508
Mol. weight: 130.59 kDa
Ligands: IHP
Released: 26 Mar 2014

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

Secondary structure: helices and β-sheets

4HNW contains 62 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: 53 helices, 0 β-strands

Element	Residues	Length
α-helix	17-32	16
α-helix	36-49	14
α-helix	54-67	14
α-helix	70-82	13
α-helix	91-103	13
α-helix	107-119	13
α-helix	127-137	11
α-helix	141-154	14
α-helix	159-171	13
α-helix	175-189	15
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	434-445	12
α-helix	446-448	3
α-helix	452-464	13
α-helix	468-475	8
α-helix	488-493	6
α-helix	497-519	23
α-helix	535-558	24
α-helix	560-570	11
α-helix	575-582	8
α-helix	585-595	11
α-helix	598-600	3
α-helix	602-624	23
α-helix	648-669	22
α-helix	674-676	3
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	714-724	11
α-helix	727-741	15
α-helix	746-759	14
α-helix	765-773	9
α-helix	774-777	4
α-helix	810-817	8
α-helix	827-834	8
α-helix	843-848	6
α-helix	849-853	5

Chain B: 9 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	1
α-helix	10-12	3
α-helix	13-23	11
α-helix	30-37	8
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	129-144	16
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

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

>4HNW_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

>4HNW_2 N-terminal acetyltransferase A complex catalytic subunit ARD1 (chains B)
MPINIRRATINDIICMQNANLHNLPENYMMKYYMYHILSWPEASFVATTTTLDCEDSDEQ
DENDKLELTLDGTNDGRTIKLDPTYLAPGEKLVGYVLVKMNDDPDQQNEPPNGHITSLSV
MRTYRRMGIAENLMRQALFALREVHQAEYVSLHVRQSNRAALHLYRDTLAFEVLSIEKSY
YQDGEDAYAMKKVLKLEELQISNFTHRRLKENEEKLEDDLESDLLEDIIKQGVNDIIVEQ
KLISEEDL

Ligands and cofactors

ID	Name	Formula	Copies
IHP	Inositol hexakisphosphate	C6 H18 O24 P6	1

Water and common crystallization additives (PG4) are not listed.

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
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
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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