Crystal Structure of the Fe-S Domain of the yeast DNA primase. Determined by X-ray diffraction at 1.54 Å resolution. Released 21 Apr 2010.
Explore 3LGB in 3D Show helices and sheets RCSB PDB PDBe
3LGB contains 31 α-helices and 0 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 | 323-325 | 3 | |
| α-helix | 327-330 | 4 | |
| α-helix | 335-347 | 13 | |
| α-helix | 352-364 | 13 | |
| α-helix | 369-379 | 11 | |
| α-helix | 388-394 | 7 | |
| α-helix | 396-402 | 7 | |
| α-helix | 412-415 | 4 | |
| α-helix | 417-422 | 6 | |
| α-helix | 424-426 | 3 | |
| α-helix | 435-438 | 4 | |
| α-helix | 441-450 | 10 | |
| α-helix | 455-466 | 12 | |
| α-helix | 470-481 | 12 | |
| α-helix | 500-510 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 323-325 | 3 | |
| α-helix | 327-330 | 4 | |
| α-helix | 335-347 | 13 | |
| α-helix | 352-364 | 13 | |
| α-helix | 369-379 | 11 | |
| α-helix | 388-390 | 3 | |
| α-helix | 391-395 | 5 | |
| α-helix | 396-402 | 7 | |
| α-helix | 412-415 | 4 | |
| α-helix | 417-422 | 6 | |
| α-helix | 424-426 | 3 | |
| α-helix | 435-438 | 4 | |
| α-helix | 441-450 | 10 | |
| α-helix | 455-466 | 12 | |
| α-helix | 470-482 | 13 | |
| α-helix | 500-509 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| DNA primase large subunit | A, B | protein | 194 | Saccharomyces cerevisiae | P20457 (AlphaFold model) |
>3LGB_1 DNA primase large subunit (chains A, B) SDEINAQSVWSEEISSNYPLCIKNLMEGLKKNHHLRYYGRQQLSLFLKGIGLSADEALKF WSEAFTNMTMEKFNKEYRYSFRHNYGLEGNRINYKPWDCHTILSKPRPGRGDYHGCPFRD WSHERLSAELRSMKLTQAQIISVLDSCQKGEYTIACTKVFEMTHNSASADLEIGEQTHIA HPNLYFERSRQLQK
Water and common crystallization additives (EPE, GOL) are not listed.
Shared Active Site Architecture between the Large Subunit of Eukaryotic Primase and DNA Photolyase. Sauguet, L., Klinge, S., Perera, R.L. et al. PLoS One (2010) 5:10083-10083. DOI 10.1371/journal.pone.0010083 · PubMed
Other PDB entries of the same protein (UniProt P20457 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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