Homo sapiens
| Assembly | Physical composition | Protein state | Molecular copy count | Associated components | Data consistency |
|---|---|---|---|---|---|
| 1 | Protein monomer | Monomer | Protein 1 | water × 1 | Consistent with protein count |
| UniProt name | ATOX1_HUMAN |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–67； UniProt 2–68 |
Homo sapiens
| Assembly | Physical composition | Protein state | Molecular copy count | Associated components | Data consistency |
|---|---|---|---|---|---|
| 2 | Protein monomer | Monomer | Protein 1 | CADMIUM ION × 1 water × 1 | Consistent with protein count |
| UniProt name | ATP7A_HUMAN |
| Isoform | — |
| PDB entities | 2 |
| Chains and sequence ranges | Author chain B； PDBConstruct 1–71； UniProt 7–77 |
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 | 3cjk |
| Deposition date deposition_date | 2008-03-13 |
| Structure title title | Crystal structure of the adduct HAH1-Cd(II)-MNK1. |
| Keywords keywords | ;HAH1; ATP7A; ATP7B; Menkes disease; metal homeostasis, Chaperone, Copper, Copper transport, Ion transport, Metal-binding, Transport, Alternative splicing, ATP-binding, Cytoplasm, Disease mutation, Endoplasmic reticulum, Glycoprotein, Golgi apparatus, Hydrolase, Magnesium, Membrane, Nucleotide-binding, Phosphoprotein, Polymorphism, Transmembrane, METAL TRANSPORT-HYDROLASE COMPLEX ;; METAL TRANSPORT/HYDROLASE |
| 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） | 12.11 Å |
| Rg (electron density) | 10.64 Å |
| Total Rg | 12.16 Å |
| Atom count | 513 |
| Residues | 68 |
| Excluded volume | 9278 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d3cjka1 |
| Class class | d — Alpha and beta proteins (a+b) |
| Fold Fold fold | d.58 — Ferredoxin-like |
| Superfamily Superfamily superfamily | d.58.17 — HMA, heavy metal-associated domain |
| Family Family family | d.58.17.1 — HMA, heavy metal-associated domain |
| Domain ID domain_id | d3cjka2 |
| Class class | l — Artifacts |
| Fold Fold fold | l.1 — Tags |
| Superfamily Superfamily superfamily | l.1.1 — Tags |
| Family Family family | l.1.1.1 — Tags |
| Domain ID domain_id | d3cjkb1 |
| Class class | d — Alpha and beta proteins (a+b) |
| Fold Fold fold | d.58 — Ferredoxin-like |
| Superfamily Superfamily superfamily | d.58.17 — HMA, heavy metal-associated domain |
| Family Family family | d.58.17.1 — HMA, heavy metal-associated domain |
| Domain ID domain_id | d3cjkb2 |
| Class class | l — Artifacts |
| Fold Fold fold | l.1 — Tags |
| Superfamily Superfamily superfamily | l.1.1 — Tags |
| Family Family family | l.1.1.1 — Tags |
| Domain ID domain_id | 3cjkA00 |
| Class class | 3 — Alpha Beta |
| Architecture architecture | 30 — 2-Layer Sandwich |
| Topology topology | 70 — Alpha-Beta Plaits |
| Homologous superfamily homologous superfamily | 100 — |
| Domain ID domain_id | 3cjkB00 |
| Class class | 3 — Alpha Beta |
| Architecture architecture | 30 — 2-Layer Sandwich |
| Topology topology | 70 — Alpha-Beta Plaits |
| Homologous superfamily homologous superfamily | 100 — |