LEUCINE-SPECIFIC BINDING PROTEIN
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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count | Chain A; UniProt 24–369 | Not recorded | LEU LEUCINE × 1 | X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.6;PEG 4000, SODIUM CITRATE, PH 5.6, 2-PROPANOL | Resolution 2.00 Å R-free 0.252 |
| 2 | Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count | Chain B; UniProt 24–369 | Not recorded | LEU LEUCINE × 1 | X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.6;PEG 4000, SODIUM CITRATE, PH 5.6, 2-PROPANOL | Resolution 2.00 Å R-free 0.252 |
| 3 | Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count | Chain C; UniProt 24–369 | Not recorded | LEU LEUCINE × 1 | X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.6;PEG 4000, SODIUM CITRATE, PH 5.6, 2-PROPANOL | Resolution 2.00 Å R-free 0.252 |
| 4 | Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count | Chain D; UniProt 24–369 | Not recorded | LEU LEUCINE × 1 | X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.6;PEG 4000, SODIUM CITRATE, PH 5.6, 2-PROPANOL | Resolution 2.00 Å R-free 0.252 |
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.
4 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states
View Construct and Data Evidence
| UniProt name | LIVK_ECOLI |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A; PDBConstruct 1–346; UniProt 24–369 Author chain B; PDBConstruct 1–346; UniProt 24–369 Author chain C; PDBConstruct 1–346; UniProt 24–369 Author chain D; PDBConstruct 1–346; UniProt 24–369 |