HOMO SAPIENS
| Assembly | Physical composition | Protein state | Molecular copy count | Associated components | Data consistency |
|---|---|---|---|---|---|
| 1 | Protein monomer | Monomer | Protein 1 | ACETIC ACID × 1 SULFATE ION × 1 water × 1 | Consistent with protein count |
| UniProt name | TBCA_HUMAN |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 2–108； UniProt 1–107 |
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 | 1h7c |
| Deposition date deposition_date | 2001-07-04 |
| Structure title title | human tubulin chaperone cofactor a |
| Keywords keywords | CHAPERONE, TUBULIN, PROTEIN FOLDING, COFACTOR A, P14; CHAPERONE |
| Experimental Method method | X-RAY DIFFRACTION |
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） | 19.78 Å |
| Rg (electron density) | 19.50 Å |
| Total Rg | 19.92 Å |
| Atom count | 874 |
| Residues | 99 |
| Excluded volume | 15641 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d1h7ca_ |
| Class class | a — All alpha proteins |
| Fold Fold fold | a.7 — Spectrin repeat-like |
| Superfamily Superfamily superfamily | a.7.5 — Tubulin chaperone cofactor A |
| Family Family family | a.7.5.1 — Tubulin chaperone cofactor A |
| Domain ID domain_id | 1h7cA00 |
| Class class | 1 — Mainly Alpha |
| Architecture architecture | 20 — Up-down Bundle |
| Topology topology | 58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1 |
| Homologous superfamily homologous superfamily | 90 — |