Lysine-specific demethylase 2B
Homo sapiens
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 607–723 | Fragment:UNP Residues 607-723 | ZN ZINC ION × 4 UNX UNKNOWN LIGAND × 6 | X-RAY DIFFRACTION X-ray crystallization conditions:sitting drop;pH 8.5;291 K;25% PEG 8000, 0.2 M sodium chloride, 0.1 M tris, pH 8.5, sitting drop, temperature 291K | Resolution 2.13 Å R-free 0.220 |
| 2 | Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count | Chain B; UniProt 607–723 | Fragment:UNP Residues 607-723 | ZN ZINC ION × 4 UNX UNKNOWN LIGAND × 4 | X-RAY DIFFRACTION X-ray crystallization conditions:sitting drop;pH 8.5;291 K;25% PEG 8000, 0.2 M sodium chloride, 0.1 M tris, pH 8.5, sitting drop, temperature 291K | Resolution 2.13 Å R-free 0.220 |
| 3 | Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count | Chain C; UniProt 607–723 | Fragment:UNP Residues 607-723 | ZN ZINC ION × 4 UNX UNKNOWN LIGAND × 4 | X-RAY DIFFRACTION X-ray crystallization conditions:sitting drop;pH 8.5;291 K;25% PEG 8000, 0.2 M sodium chloride, 0.1 M tris, pH 8.5, sitting drop, temperature 291K | Resolution 2.13 Å R-free 0.220 |
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.
2 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states
View Construct and Data Evidence
| UniProt name | KDM2B_HUMAN |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A; PDBConstruct 2–118; UniProt 607–723 Author chain B; PDBConstruct 2–118; UniProt 607–723 Author chain C; PDBConstruct 2–118; UniProt 607–723 |