DNA replication regulator SLD3
Saccharomyces cerevisiae
State in the Current Structure
| Assembly | Oligomeric State | Construct | Mutations and Modifications | Ligands, Ions and Associated Components | Method and Experimental Conditions | Structure Quality |
|---|---|---|---|---|---|---|
| 1 | Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count | Chain A; UniProt 148–430 | Fragment:UNP RESIDUES 148-430 | SO4 SULFATE ION × 1 EDO 1,2-ETHANEDIOL × 16 | X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.4;293 K;PEG 4000, LiSO4, pH 8.4, vapor diffusion, hanging drop, temperature 293K | Resolution 2.40 Å R-free 0.262 |
| 2 | Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count | Chain B; UniProt 148–430 | Fragment:UNP RESIDUES 148-430 | SO4 SULFATE ION × 1 EDO 1,2-ETHANEDIOL × 8 | X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.4;293 K;PEG 4000, LiSO4, pH 8.4, vapor diffusion, hanging drop, temperature 293K | Resolution 2.40 Å R-free 0.262 |
| 3 | Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count | Chain C; UniProt 148–430 | Fragment:UNP RESIDUES 148-430 | SO4 SULFATE ION × 1 | X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.4;293 K;PEG 4000, LiSO4, pH 8.4, vapor diffusion, hanging drop, temperature 293K | Resolution 2.40 Å R-free 0.262 |
Other States of the Same Protein in the Database
Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.
5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states
View Construct and Data Evidence
| UniProt name | SLD3_YEAST |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A; PDBConstruct 2–284; UniProt 148–430 Author chain B; PDBConstruct 2–284; UniProt 148–430 Author chain C; PDBConstruct 2–284; UniProt 148–430 |