Crystal structure of yeast N-terminal acetyltransferase NatE (IP6) in complex with a bisubstrate. Determined by X-ray diffraction at 2.1 Å resolution. Released 20 Jul 2016.
Explore 4XNH in 3D Show helices and sheets RCSB PDB PDBe
4XNH contains 67 α-helices and 16 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 24-32 | 9 | |
| α-helix | 36-49 | 14 | |
| α-helix | 54-66 | 13 | |
| α-helix | 70-83 | 14 | |
| α-helix | 91-103 | 13 | |
| α-helix | 107-119 | 13 | |
| α-helix | 126-138 | 13 | |
| 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 | 275-284 | 10 | |
| α-helix | 291-304 | 14 | |
| α-helix | 309-313 | 5 | |
| α-helix | 314-317 | 4 | |
| α-helix | 322-339 | 18 | |
| α-helix | 344-354 | 11 | |
| α-helix | 356-372 | 17 | |
| α-helix | 380-396 | 17 | |
| α-helix | 400-413 | 14 | |
| α-helix | 418-431 | 14 | |
| α-helix | 434-447 | 14 | |
| α-helix | 452-464 | 13 | |
| α-helix | 468-475 | 8 | |
| α-helix | 488-493 | 6 | |
| α-helix | 497-523 | 27 | |
| α-helix | 536-570 | 35 | |
| α-helix | 571-574 | 4 | |
| α-helix | 575-582 | 8 | |
| α-helix | 585-595 | 11 | |
| α-helix | 598-600 | 3 | |
| α-helix | 602-621 | 20 | |
| α-helix | 662-669 | 8 | |
| α-helix | 683-686 | 4 | |
| α-helix | 691-695 | 5 | |
| α-helix | 696-700 | 5 | |
| α-helix | 701-706 | 6 | |
| α-helix | 714-721 | 8 | |
| α-helix | 727-741 | 15 | |
| α-helix | 746-758 | 13 | |
| α-helix | 767-781 | 15 | |
| α-helix | 787-791 | 5 | |
| α-helix | 797-805 | 9 | |
| α-helix | 810-818 | 9 | |
| α-helix | 827-837 | 11 | |
| α-helix | 843-848 | 6 | |
| α-helix | 849-853 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-7 | 5 | 1 |
| α-helix | 10-12 | 3 | |
| α-helix | 13-23 | 11 | |
| α-helix | 30-39 | 10 | |
| β-strand | 45-49 | 5 | 1 |
| β-strand | 85-87 | 3 | 2 |
| β-strand | 90-91 | 2 | 2 |
| β-strand | 92-100 | 9 | 1 |
| 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 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 6-9 | 4 | 3 |
| α-helix | 13-15 | 3 | |
| α-helix | 16-26 | 11 | |
| α-helix | 33-39 | 7 | |
| β-strand | 59-66 | 8 | 3 |
| β-strand | 69-79 | 11 | 3 |
| β-strand | 90-98 | 9 | 3 |
| α-helix | 100-102 | 3 | |
| α-helix | 107-121 | 15 | |
| β-strand | 126-132 | 7 | 3 |
| α-helix | 136-144 | 9 | |
| β-strand | 148-159 | 12 | 3 |
| β-strand | 165-174 | 10 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| N-terminal acetyltransferase A complex subunit NAT1 | A | protein | 854 | Saccharomyces cerevisiae | P12945 (AlphaFold model) |
| N-terminal acetyltransferase A complex catalytic subunit ARD1 | B | protein | 238 | Saccharomyces cerevisiae | P07347 (AlphaFold model) |
| N-terminal acetyltransferase A complex subunit NAT5 | C | protein | 176 | Saccharomyces cerevisiae | Q08689 (AlphaFold model) |
| ACYH8 | F | protein | 8 | Homo sapiens | P01189 (AlphaFold model) |
>4XNH_1 N-terminal acetyltransferase A complex subunit NAT1 (chains A) MSRKRSTKPKPAAKIALKKENDQFLEALKLYEGKQYKKSLKLLDAILKKDGSHVDSLALK GLDLYSVGEKDDAASYVANAIRKIEGASASPICCHVLGIYMRNTKEYKESIKWFTAALNN GSTNKQIYRDLATLQSQIGDFKNALVSRKKYWEAFLGYRANWTSLAVAQDVNGERQQAIN TLSQFEKLAEGKISDSEKYEHSECLMYKNDIMYKAASDNQDKLQNVLKHLNDIEPCVFDK FGLLERKATIYMKLGQLKDASIVYRTLIKRNPDNFKYYKLLEVSLGIQGDNKLKKALYGK LEQFYPRCEPPKFIPLTFLQDKEELSKKLREYVLPQLERGVPATFSNVKPLYQRRKSKVS PLLEKIVLDYLSGLDPTQDPIPFIWTNYYLSQHFLFLKDFPKAQEYIDAALDHTPTLVEF YILKARILKHLGLMDTAAGILEEGRQLDLQDRFINCKTVKYFLRANNIDKAVEVASLFTK NDDSVNGIKDLHLVEASWFIVEQAEAYYRLYLDRKKKLDDLASLKKEVESDKSEQIANDI KENQWLVRKYKGLALKRFNAIPKFYKQFEDDQLDFHSYCMRKGTPRAYLEMLEWGKALYT KPMYVRAMKEASKLYFQMHDDRLKRKSDSLDENSDEIQNNGQNSSSQKKKAKKEAAAMNK RKETEAKSVAAYPSDQDNDVFGEKLIETSTPMEDFATEFYNNYSMQVREDERDYILDFEF NYRIGKLALCFASLNKFAKRFGTTSGLFGSMAIVLLHATRNDTPFDPILKKVVTKSLEKE YSENFPLNEISNNSFDWLNFYQEKFGKNDINGLLFLYRYRDDVPIGSSNLKEMIISSLSP LEPHSQNEILQYYL
>4XNH_2 N-terminal acetyltransferase A complex catalytic subunit ARD1 (chains B) MPINIRRATINDIICMQNANLHNLPENYMMKYYMYHILSWPEASFVATTTTLDCEDSDEQ DENDKLELTLDGTNDGRTIKLDPTYLAPGEKLVGYVLVKMNDDPDQQNEPPNGHITSLSV MRTYRRMGIAENLMRQALFALREVHQAEYVSLHVRQSNRAALHLYRDTLAFEVLSIEKSY YQDGEDAYAMKKVLKLEELQISNFTHRRLKENEEKLEDDLESDLLEDIIKQGVNDIIV
>4XNH_3 N-terminal acetyltransferase A complex subunit NAT5 (chains C) MGRDICTLDNVYANNLGMLTKLAHVTVPNLYQDAFFSALFAEDSLVAKNKKPSSKKDVHF TQMAYYSEIPVGGLVAKLVPKKQNELSLKGIQIEFLGVLPNYRHKSIGSKLLKFAEDKCS ECHQHNVFVYLPAVDDLTKQWFIAHGFEQVGETVNNFIKGVNGDEQDAILLKKHIS
>4XNH_4 ACYH8 (chains F) SYSMEHFR
| ID | Name | Formula | Copies |
|---|---|---|---|
| IHP | Inositol hexakisphosphate | C6 H18 O24 P6 | 1 |
| ACO | Acetyl coenzyme *a | C23 H38 N7 O17 P3 S | 1 |
| CMC | Carboxymethyl coenzyme *a | C23 H38 N7 O18 P3 S | 1 |
Crystal structure of yeast N-terminal acetyltransferase NatE (IP6) in complex with a bisubstrate. Dong, J., Wang, S., York, J.D. To be published.
Other PDB entries of the same protein (UniProt P12945 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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