Crystal structure of yeast N-terminal acetyltransferase NatE (ppGpp) in complex with a bisubstrate. Determined by X-ray diffraction at 2.81 Å resolution. Released 20 Jul 2016.
Explore 4XPD in 3D Show helices and sheets RCSB PDB PDBe
4XPD contains 66 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 23-32 | 10 | |
| α-helix | 36-49 | 14 | |
| α-helix | 54-67 | 14 | |
| α-helix | 70-81 | 12 | |
| 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 | 175-188 | 14 | |
| α-helix | 195-197 | 3 | |
| α-helix | 198-216 | 19 | |
| α-helix | 220-233 | 14 | |
| α-helix | 234-236 | 3 | |
| α-helix | 240-254 | 15 | |
| α-helix | 257-270 | 14 | |
| α-helix | 275-284 | 10 | |
| α-helix | 291-304 | 14 | |
| α-helix | 310-313 | 4 | |
| 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 | 418-430 | 13 | |
| α-helix | 434-445 | 12 | |
| α-helix | 452-464 | 13 | |
| α-helix | 468-475 | 8 | |
| α-helix | 476-478 | 3 | |
| α-helix | 488-493 | 6 | |
| α-helix | 497-523 | 27 | |
| α-helix | 536-570 | 35 | |
| α-helix | 575-582 | 8 | |
| α-helix | 585-595 | 11 | |
| α-helix | 598-600 | 3 | |
| α-helix | 602-623 | 22 | |
| α-helix | 666-669 | 4 | |
| 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 | 727-740 | 14 | |
| α-helix | 746-759 | 14 | |
| α-helix | 774-780 | 7 | |
| α-helix | 797-804 | 8 | |
| α-helix | 810-818 | 9 | |
| α-helix | 827-836 | 10 | |
| 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 | 30-37 | 8 | |
| β-strand | 45-49 | 5 | 1 |
| β-strand | 85 | 1 | 2 |
| β-strand | 91 | 1 | 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 | 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 | 33-40 | 8 | |
| β-strand | 58-66 | 9 | 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 | 148-149 | 2 | 3 |
| β-strand | 154-159 | 6 | 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) |
| human ACTH8 | F | protein | 8 | Homo sapiens | P01189 (AlphaFold model) |
>4XPD_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
>4XPD_2 N-terminal acetyltransferase A complex catalytic subunit ARD1 (chains B) MPINIRRATINDIICMQNANLHNLPENYMMKYYMYHILSWPEASFVATTTTLDCEDSDEQ DENDKLELTLDGTNDGRTIKLDPTYLAPGEKLVGYVLVKMNDDPDQQNEPPNGHITSLSV MRTYRRMGIAENLMRQALFALREVHQAEYVSLHVRQSNRAALHLYRDTLAFEVLSIEKSY YQDGEDAYAMKKVLKLEELQISNFTHRRLKENEEKLEDDLESDLLEDIIKQGVNDIIV
>4XPD_3 N-terminal acetyltransferase A complex subunit NAT5 (chains C) MGRDICTLDNVYANNLGMLTKLAHVTVPNLYQDAFFSALFAEDSLVAKNKKPSSKKDVHF TQMAYYSEIPVGGLVAKLVPKKQNELSLKGIQIEFLGVLPNYRHKSIGSKLLKFAEDKCS ECHQHNVFVYLPAVDDLTKQWFIAHGFEQVGETVNNFIKGVNGDEQDAILLKKHIS
>4XPD_4 human ACTH8 (chains F) SYSMEHFR
| ID | Name | Formula | Copies |
|---|---|---|---|
| CMC | Carboxymethyl coenzyme *a | C23 H38 N7 O18 P3 S | 1 |
| ACO | Acetyl coenzyme *a | C23 H38 N7 O17 P3 S | 1 |
| G4P | Guanosine-5',3'-tetraphosphate | C10 H17 N5 O17 P4 | 1 |
Crystal structure of yeast N-terminal acetyltransferase NatE (ppGpp) 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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