3LGB: Fe-S Domain of the yeast DNA primase

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.

Method
X-ray diffraction
Resolution
1.54 Å
Organism
Saccharomyces cerevisiae
Chains
2
Atoms
3,704
Mol. weight
47.29 kDa
Ligands
SF4, ZN
Released
21 Apr 2010

Explore 3LGB in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 15 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix323-3253
α-helix327-3304
α-helix335-34713
α-helix352-36413
α-helix369-37911
α-helix388-3947
α-helix396-4027
α-helix412-4154
α-helix417-4226
α-helix424-4263
α-helix435-4384
α-helix441-45010
α-helix455-46612
α-helix470-48112
α-helix500-51011
Chain B: 16 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix323-3253
α-helix327-3304
α-helix335-34713
α-helix352-36413
α-helix369-37911
α-helix388-3903
α-helix391-3955
α-helix396-4027
α-helix412-4154
α-helix417-4226
α-helix424-4263
α-helix435-4384
α-helix441-45010
α-helix455-46612
α-helix470-48213
α-helix500-50910

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
DNA primase large subunitA, Bprotein194Saccharomyces cerevisiaeP20457 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>3LGB_1 DNA primase large subunit (chains A, B)
SDEINAQSVWSEEISSNYPLCIKNLMEGLKKNHHLRYYGRQQLSLFLKGIGLSADEALKF
WSEAFTNMTMEKFNKEYRYSFRHNYGLEGNRINYKPWDCHTILSKPRPGRGDYHGCPFRD
WSHERLSAELRSMKLTQAQIISVLDSCQKGEYTIACTKVFEMTHNSASADLEIGEQTHIA
HPNLYFERSRQLQK

Ligands and cofactors

IDNameFormulaCopies
SF4Iron/sulfur clusterFe4 S42
ZNZinc ionZn2

Water and common crystallization additives (EPE, GOL) are not listed.

Primary citation

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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