Structure of the S. cerevisiae clamp loader Replication Factor C (RFC) with mixed nucleotide occupancy. Determined by electron microscopy at 2.57 Å resolution. Released 12 Nov 2025.
Explore 9PEO in 3D Show helices and sheets RCSB PDB PDBe
9PEO contains 113 α-helices and 33 β-strands across 5 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 | 545-558 | 14 | |
| β-strand | 560 | 1 | 1 |
| α-helix | 562-564 | 3 | |
| α-helix | 566-571 | 6 | |
| α-helix | 574-582 | 9 | |
| α-helix | 588-595 | 8 | |
| β-strand | 599-601 | 3 | 1 |
| α-helix | 604-605 | 2 | |
| α-helix | 610-632 | 23 | |
| α-helix | 638-640 | 3 | |
| α-helix | 641-645 | 5 | |
| α-helix | 646-650 | 5 | |
| α-helix | 651-655 | 5 | |
| β-strand | 658-660 | 3 | 1 |
| α-helix | 665-667 | 3 | |
| α-helix | 669-690 | 22 | |
| α-helix | 698-700 | 3 | |
| α-helix | 701-705 | 5 | |
| α-helix | 706-713 | 8 | |
| α-helix | 715-720 | 6 | |
| α-helix | 721-724 | 4 | |
| α-helix | 725-733 | 9 | |
| α-helix | 739-745 | 7 | |
| α-helix | 746-748 | 3 | |
| α-helix | 751-753 | 3 | |
| α-helix | 756-761 | 6 | |
| α-helix | 764-775 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 11-14 | 4 | |
| α-helix | 20-22 | 3 | |
| α-helix | 27-39 | 13 | |
| α-helix | 42-44 | 3 | |
| β-strand | 45-49 | 5 | 2 |
| α-helix | 55-66 | 12 | |
| α-helix | 68-70 | 3 | |
| α-helix | 71-74 | 4 | |
| β-strand | 75-79 | 5 | 2 |
| α-helix | 86-97 | 12 | |
| β-strand | 109-114 | 6 | 2 |
| α-helix | 116-118 | 3 | |
| α-helix | 121-133 | 13 | |
| β-strand | 138-144 | 7 | 2 |
| α-helix | 152-157 | 6 | |
| β-strand | 159-163 | 5 | 2 |
| α-helix | 165-167 | 3 | |
| α-helix | 168-182 | 15 | |
| β-strand | 186 | 1 | 3 |
| α-helix | 188-197 | 10 | |
| α-helix | 202-216 | 15 | |
| β-strand | 219 | 1 | 3 |
| α-helix | 221-227 | 7 | |
| α-helix | 231-232 | 2 | |
| α-helix | 233-241 | 9 | |
| α-helix | 245-251 | 7 | |
| α-helix | 252-257 | 6 | |
| α-helix | 263-275 | 13 | |
| α-helix | 282-300 | 19 | |
| α-helix | 306-321 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 31-43 | 13 | |
| β-strand | 49-52 | 4 | 4 |
| α-helix | 59-70 | 12 | |
| α-helix | 75-78 | 4 | |
| β-strand | 79-83 | 5 | 4 |
| α-helix | 84-86 | 3 | |
| α-helix | 90-102 | 13 | |
| β-strand | 112-117 | 6 | 4 |
| α-helix | 119-121 | 3 | |
| α-helix | 124-136 | 13 | |
| β-strand | 141-147 | 7 | 4 |
| α-helix | 150-152 | 3 | |
| α-helix | 155-159 | 5 | |
| β-strand | 162-165 | 4 | 4 |
| α-helix | 166-170 | 5 | |
| α-helix | 171-185 | 15 | |
| β-strand | 188-189 | 2 | 5 |
| α-helix | 191-201 | 11 | |
| α-helix | 205-218 | 14 | |
| β-strand | 226-227 | 2 | 5 |
| α-helix | 228 | 1 | |
| α-helix | 229-236 | 8 | |
| α-helix | 241-253 | 13 | |
| α-helix | 256-269 | 14 | |
| α-helix | 274-286 | 13 | |
| α-helix | 293-311 | 19 | |
| α-helix | 316-330 | 15 | |
| α-helix | 331-333 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 27-30 | 4 | |
| α-helix | 36-38 | 3 | |
| α-helix | 43-54 | 12 | |
| β-strand | 60-64 | 5 | 6 |
| α-helix | 71-82 | 12 | |
| α-helix | 87-89 | 3 | |
| β-strand | 92-96 | 5 | 6 |
| α-helix | 103-115 | 13 | |
| α-helix | 117-121 | 5 | |
| α-helix | 123-128 | 6 | |
| β-strand | 135-140 | 6 | 6 |
| α-helix | 142-144 | 3 | |
| α-helix | 147-159 | 13 | |
| β-strand | 164-170 | 7 | 6 |
| α-helix | 173-175 | 3 | |
| α-helix | 178-182 | 5 | |
| β-strand | 184-188 | 5 | 6 |
| α-helix | 189-193 | 5 | |
| α-helix | 194-207 | 14 | |
| β-strand | 212 | 1 | 7 |
| α-helix | 216-224 | 9 | |
| α-helix | 228-244 | 17 | |
| α-helix | 249-250 | 2 | |
| β-strand | 251 | 1 | 7 |
| α-helix | 253-260 | 8 | |
| α-helix | 265-277 | 13 | |
| α-helix | 280-291 | 12 | |
| α-helix | 297-309 | 13 | |
| α-helix | 316-333 | 18 | |
| α-helix | 339-351 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-7 | 4 | |
| α-helix | 13-15 | 3 | |
| α-helix | 20-30 | 11 | |
| α-helix | 36-38 | 3 | |
| β-strand | 39-42 | 4 | 8 |
| α-helix | 49-60 | 12 | |
| α-helix | 63-66 | 4 | |
| β-strand | 69-76 | 8 | 8 |
| α-helix | 78-80 | 3 | |
| β-strand | 82-89 | 8 | 8 |
| β-strand | 93-96 | 4 | 8 |
| α-helix | 98-104 | 7 | |
| α-helix | 105-119 | 15 | |
| β-strand | 136-141 | 6 | 8 |
| α-helix | 143-145 | 3 | |
| α-helix | 148-160 | 13 | |
| β-strand | 165-171 | 7 | 8 |
| α-helix | 179-184 | 6 | |
| β-strand | 186-189 | 4 | 8 |
| α-helix | 191-194 | 4 | |
| α-helix | 195-209 | 15 | |
| β-strand | 212-213 | 2 | 9 |
| α-helix | 217-226 | 10 | |
| α-helix | 230-243 | 14 | |
| β-strand | 247-248 | 2 | 9 |
| α-helix | 252-255 | 4 | |
| α-helix | 258-272 | 15 | |
| α-helix | 276-291 | 16 | |
| α-helix | 296-307 | 12 | |
| α-helix | 315-333 | 19 | |
| α-helix | 338-353 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Replication factor C subunit 1 | A | protein | 861 | Saccharomyces cerevisiae | P38630 (AlphaFold model) |
| Replication factor C subunit 4 | B | protein | 323 | Saccharomyces cerevisiae | P40339 (AlphaFold model) |
| Replication factor C subunit 3 | C | protein | 340 | Saccharomyces cerevisiae | P38629 (AlphaFold model) |
| Replication factor C subunit 2 | D | protein | 353 | Saccharomyces cerevisiae | P40348 (AlphaFold model) |
| Replication factor C subunit 5 | E | protein | 354 | Saccharomyces cerevisiae | P38251 |
>9PEO_1 Replication factor C subunit 1 (chains A) MVNISDFFGKNKKSVRSSTSRPTRQVGSSKPEVIDLDTESDQESTNKTPKKMPVSNVIDV SETPEGEKKLPLPAKRKASSPTVKPASSKKTKPSSKSSDSASNITAQDVLDKIPSLDLSN VHVKENAKFDFKSANSNADPDEIVSEIGSFPEGKPNCLLGLTIVFTGVLPTLERGASEAL AKRYGARVTKSISSKTSVVVLGDEAGPKKLEKIKQLKIKAIDEEGFKQLIAGMPAEGGDG EAAEKARRKLEEQHNIATKEAELLVKKEEERSKKLAATRVSGGHLERDNVVREEDKLWTV KYAPTNLQQVCGNKGSVMKLKNWLANWENSKKNSFKHAGKDGSGVFRAAMLYGPPGIGKT TAAHLVAQELGYDILEQNASDVRSKTLLNAGVKNALDNMSVVGYFKHNEEAQNLNGKHFV IIMDEVDGMSGGDRGGVGQLAQFCRKTSTPLILICNERNLPKMRPFDRVCLDIQFRRPDA NSIKSRLMTIAIREKFKLDPNVIDRLIQTTRGDIRQVINLLSTISTTTKTINHENINEIS KAWEKNIALKPFDIAHKMLDGQIYSDIGSRNFTLNDKIALYFDDFDFTPLMIQENYLSTR PSVLKPGQSHLEAVAEAANCISLGDIVEKKIRSSEQLWSLLPLHAVLSSVYPASKVAGHM AGRINFTAWLGQNSKSAKYYRLLQEIHYHTRLGTSTDKIGLRLDYLPTFRKRLLDPFLKQ GADAISSVIEVMDDYYLTKEDWDSIMEFFVGPDVTTAIIKKIPATVKSGFTRKYNSMTHP VAIYRTGSTIGGGGVGTSTSTPDFEDVVDADDNPVPADDEETQDSSTDLKKDKLIKQKAK PTKRKTATSKPGGSKKRKTKA
>9PEO_2 Replication factor C subunit 4 (chains B) MSKTLSLQLPWVEKYRPQVLSDIVGNKETIDRLQQIAKDGNMPHMIISGMPGIGKTTSVH CLAHELLGRSYADGVLELNASDDRGIDVVRNQIKHFAQKKLHLPPGKHKIVILDEADSMT AGAQQALRRTMELYSNSTRFAFACNQSNKIIEPLQSRCAILRYSKLSDEDVLKRLLQIIK LEDVKYTNDGLEAIIFTAEGDMRQAINNLQSTVAGHGLVNADNVFKIVDSPHPLIVKKML LASNLEDSIQILRTDLWKKGYSSIDIVTTSFRVTKNLAQVKESVRLEMIKEIGLTHMRIL EGVGTYLQLASMLAKIHKLNNKA
>9PEO_3 Replication factor C subunit 3 (chains C) MSTSTEKRSKENLPWVEKYRPETLDEVYGQNEVITTVRKFVDEGKLPHLLFYGPPGTGKT STIVALAREIYGKNYSNMVLELNASDDRGIDVVRNQIKDFASTRQIFSKGFKLIILDEAD AMTNAAQNALRRVIERYTKNTRFCVLANYAHKLTPALLSRCTRFRFQPLPQEAIERRIAN VLVHEKLKLSPNAEKALIELSNGDMRRVLNVLQSCKATLDNPDEDEISDDVIYECCGAPR PSDLKAVLKSILEDDWGTAHYTLNKVRSAKGLALIDLIEGIVKILEDYELQNEETRVHLL TKLADIEYSISKGGNDQIQGSAVIGAIKASFENETVKANV
>9PEO_4 Replication factor C subunit 2 (chains D) MFEGFGPNKKRKISKLAAEQSLAQQPWVEKYRPKNLDEVTAQDHAVTVLKKTLKSANLPH MLFYGPPGTGKTSTILALTKELYGPDLMKSRILELNASDERGISIVREKVKNFARLTVSK PSKHDLENYPCPPYKIIILDEADSMTADAQSALRRTMETYSGVTRFCLICNYVTRIIDPL ASRCSKFRFKALDASNAIDRLRFISEQENVKCDDGVLERILDISAGDLRRGITLLQSASK GAQYLGDGKNITSTQVEELAGVVPHDILIEIVEKVKSGDFDEIKKYVNTFMKSGWSAASV VNQLHEYYITNDNFDTNFKNQISWLLFTTDSRLNNGTNEHIQLLNLLVKISQL
>9PEO_5 Replication factor C subunit 5 (chains E) MSLWVDKYRPKSLNALSHNEELTNFLKSLSDQPRDLPHLLLYGPNGTGKKTRCMALLESI FGPGVYRLKIDVRQFVTASNRKLELNVVSSPYHLEITPSDMGNNDRIVIQELLKEVAQME QVDFQDSKDGLAHRYKCVIINEANSLTKDAQAALRRTMEKYSKNIRLIMVCDSMSPIIAP IKSRCLLIRCPAPSDSEISTILSDVVTNERIQLETKDILKRIAQASNGNLRVSLLMLESM ALNNELALKSSSPIIKPDWIIVIHKLTRKIVKERSVNSLIECRAVLYDLLAHCIPANIIL KELTFSLLDVETLNTTNKSSIIEYSSVFDERLSLGNKAIFHLEGFIAKVMCCLD
| ID | Name | Formula | Copies |
|---|---|---|---|
| GDP | Guanosine-5'-diphosphate | C10 H15 N5 O11 P2 | 1 |
| ADP | Adenosine-5'-diphosphate | C10 H15 N5 O10 P2 | 1 |
Water and common crystallization additives (ACT) are not listed.
PCNA is a nucleotide exchange factor for the clamp loader ATPase complex. Pajak, J., Landeck, J.T., Liu, X. et al. Proc Natl Acad Sci U S A (2025) 122:e2518834122-e2518834122. DOI 10.1073/pnas.2518834122 · PubMed
Other PDB entries of the same protein (UniProt P38630 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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