Histone-like protein HLP-1
Escherichia coli
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 homooligomer Homooligomer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count | Chain A; UniProt 21–161 Chain B; UniProt 21–161 Chain C; UniProt 21–161 | Non-standard monomer:Yes (specific site not provided by mmCIF) | No other associated polymer | X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;277 K;PEG 350 monomethy ether, ammonium dihydrogen phosphate, Tris, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K | Resolution 2.30 Å R-free 0.259 |
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.
1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states
View Construct and Data Evidence
| UniProt name | HLPA_ECOLI |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A; PDBConstruct 3–143; UniProt 21–161 Author chain B; PDBConstruct 3–143; UniProt 21–161 Author chain C; PDBConstruct 3–143; UniProt 21–161 |