Homo sapiens
| Assembly | Physical composition | Protein state | Molecular copy count | Associated components | Data consistency |
|---|---|---|---|---|---|
| 1 | Protein monomer | Monomer | Protein 1 | No other associated polymer | Consistent with protein count |
| UniProt name | B3AT_HUMAN |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–15； UniProt 1–15 |
The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.
| Entry ID entry_id | 2bta |
| Deposition date deposition_date | 1995-11-13 |
| Structure title title | NMR STUDY OF N-TERMINAL HUMAN BAND 3 PEPTIDE, RESIDUES 1-15 |
| Keywords keywords | ANION EXCHANGE, PHOSPHORYLATION, LIPOPROTEIN; ANION EXCHANGE |
| Experimental Method method | SOLUTION NMR |
This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.
Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)
| Rg（Guinier） | 9.67 Å |
| Rg (electron density) | 8.40 Å |
| Total Rg | 9.99 Å |
| Atom count | 238 |
| Residues | 15 |
| Excluded volume | 2211 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d2btaa_ |
| Class class | j — Peptides |
| Fold Fold fold | j.35 — Transmembrane helical fragments |
| Superfamily Superfamily superfamily | j.35.1 — Transmembrane helical fragments |
| Family Family family | j.35.1.1 — Transmembrane helical fragments |