Crystal structure of peroxisomal citrate synthase (Cit2) from Saccharomyces cerevisiae in complex with oxaloacetate and coenzyme-A. Determined by X-ray diffraction at 1.48 Å resolution. Released 26 Apr 2023.
Explore 8GR9 in 3D Show helices and sheets RCSB PDB PDBe
8GR9 contains 56 α-helices and 20 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 26-48 | 23 | |
| β-strand | 52-57 | 6 | 1 |
| α-helix | 58-61 | 4 | |
| β-strand | 69-72 | 4 | 2 |
| β-strand | 76-79 | 4 | 3 |
| β-strand | 83-86 | 4 | 3 |
| β-strand | 89 | 1 | 3 |
| α-helix | 91-97 | 7 | |
| β-strand | 100 | 1 | 4 |
| β-strand | 107 | 1 | 4 |
| α-helix | 108 | 1 | |
| α-helix | 109-118 | 10 | |
| α-helix | 121-123 | 3 | |
| α-helix | 124-136 | 13 | |
| α-helix | 139-141 | 3 | |
| α-helix | 142-150 | 9 | |
| α-helix | 157-167 | 11 | |
| α-helix | 168-171 | 4 | |
| α-helix | 173-180 | 8 | |
| α-helix | 184-186 | 3 | |
| α-helix | 187-214 | 28 | |
| α-helix | 221-223 | 3 | |
| α-helix | 228-236 | 9 | |
| α-helix | 241-253 | 13 | |
| α-helix | 262-272 | 11 | |
| α-helix | 277-288 | 12 | |
| α-helix | 296-309 | 14 | |
| α-helix | 317-329 | 13 | |
| β-strand | 337 | 1 | 5 |
| α-helix | 347-359 | 13 | |
| α-helix | 364-373 | 10 | |
| α-helix | 376-383 | 8 | |
| β-strand | 391 | 1 | 5 |
| α-helix | 394-403 | 10 | |
| α-helix | 409-411 | 3 | |
| α-helix | 412-434 | 23 | |
| α-helix | 436-439 | 4 | |
| β-strand | 442-444 | 3 | 6 |
| α-helix | 446-458 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 26-48 | 23 | |
| β-strand | 52-57 | 6 | 1 |
| α-helix | 58-61 | 4 | |
| β-strand | 69-72 | 4 | 6 |
| β-strand | 76-79 | 4 | 7 |
| β-strand | 83-86 | 4 | 7 |
| β-strand | 89 | 1 | 7 |
| α-helix | 91-97 | 7 | |
| β-strand | 100 | 1 | 8 |
| β-strand | 107 | 1 | 8 |
| α-helix | 108 | 1 | |
| α-helix | 109-118 | 10 | |
| α-helix | 121-123 | 3 | |
| α-helix | 124-136 | 13 | |
| α-helix | 139-141 | 3 | |
| α-helix | 142-150 | 9 | |
| α-helix | 157-167 | 11 | |
| α-helix | 168-171 | 4 | |
| α-helix | 173-179 | 7 | |
| α-helix | 184-186 | 3 | |
| α-helix | 187-214 | 28 | |
| α-helix | 228-236 | 9 | |
| α-helix | 241-253 | 13 | |
| α-helix | 262-272 | 11 | |
| α-helix | 277-288 | 12 | |
| α-helix | 296-310 | 15 | |
| α-helix | 317-329 | 13 | |
| β-strand | 337-339 | 3 | 9 |
| α-helix | 347-359 | 13 | |
| α-helix | 364-383 | 20 | |
| β-strand | 388-391 | 4 | 9 |
| α-helix | 394-403 | 10 | |
| α-helix | 409-411 | 3 | |
| α-helix | 412-433 | 22 | |
| α-helix | 436-439 | 4 | |
| β-strand | 442-444 | 3 | 2 |
| α-helix | 446-458 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Citrate synthase | A, B | protein | 460 | Saccharomyces cerevisiae | P08679 (AlphaFold model) |
>8GR9_1 Citrate synthase (chains A, B) MTVPYLNSNRNVASYLQSNSSQEKTLKERFSEIYPIHAQDVRQFVKEHGKTKISDVLLEQ VYGGMRGIPGSVWEGSVLDPEDGIRFRGRTIADIQKDLPKAKGSSQPLPEALFWLLLTGE VPTQAQVENLSADLMSRSELPSHVVQLLDNLPKDLHPMAQFSIAVTALESESKFAKAYAQ GISKQDYWSYTFEDSLDLLGKLPVIAAKIYRNVFKDGKMGEVDPNADYAKNLVNLIGSKD EDFVDLMRLYLTIHSDHEGGNVSAHTSHLVGSALSSPYLSLASGLNGLAGPLHGRANQEV LEWLFALKEEVNDDYSKDTIEKYLWDTLNSGRVIPGYGHAVLRKTDPRYMAQRKFAMDHF PDYELFKLVSSIYEVAPGVLTEHGKTKNPWPNVDAHSGVLLQYYGLKESSFYTVLFGVSR AFGILAQLITDRAIGASIERPKSYSTEKYKELVKNIESKL
Water and common crystallization additives (GOL, K, CL) are not listed.
Defective import of mitochondrial metabolic enzyme elicits ectopic metabolic stress. Nishio, K., Kawarasaki, T., Sugiura, Y. et al. Sci Adv (2023) 9:eadf1956-eadf1956. DOI 10.1126/sciadv.adf1956 · PubMed
Other PDB entries of the same protein (UniProt P08679 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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