Protein Mis18-alpha
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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count | Chain A; UniProt 191–233 Chain B; UniProt 191–233 | Not recorded | Protein Mis18-beta × 1 (O43482) | X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;295.15 K;Magnesium acetate, PEG 3350 | Resolution 2.50 Å R-free 0.280 |
| 2 | Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count | Chain D; UniProt 191–233 Chain E; UniProt 191–233 | Not recorded | Protein Mis18-beta × 1 (O43482) | X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;295.15 K;Magnesium acetate, PEG 3350 | Resolution 2.50 Å R-free 0.280 |
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 5 assemblies. Open the comparison page and filter oligomeric states
View Construct and Data Evidence
| UniProt name | MS18A_HUMAN |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A; PDBConstruct 4–46; UniProt 191–233 Author chain B; PDBConstruct 4–46; UniProt 191–233 Author chain D; PDBConstruct 4–46; UniProt 191–233 Author chain E; PDBConstruct 4–46; UniProt 191–233 |