Homo sapiens
| Assembly | Physical composition | Protein state | Molecular copy count | Associated components | Data consistency |
|---|---|---|---|---|---|
| 1 | Protein heterocomplex | Heteromer | Protein 2 | Complement C4-B × 1 （P0C0L5） NICKEL (II) ION × 1 | Consistent with protein count |
| UniProt name | CO2_HUMAN |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain B； PDBConstruct 1–752； UniProt 1–752 |
Homo sapiens
| Assembly | Physical composition | Protein state | Molecular copy count | Associated components | Data consistency |
|---|---|---|---|---|---|
| 1 | Protein heterocomplex | Heteromer | Protein 2 | Complement C2 × 1 （P06681） NICKEL (II) ION × 1 | Consistent with protein count |
| UniProt name | CO4B_HUMAN |
| Isoform | — |
| PDB entities | 2 |
| Chains and sequence ranges | Author chain E； PDBConstruct 1–1744； UniProt 1–1744 |
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 | 9u60 |
| Deposition date deposition_date | 2025-03-22 |
| Structure title title | C3 convertases zymogen C4b2 in loading state |
| Keywords keywords | complement system, classical passway, C3 convertases zymogen, loading state, IMMUNOSUPPRESSANT; IMMUNOSUPPRESSANT |
| Experimental Method method | ELECTRON MICROSCOPY |
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） | 48.23 Å |
| Rg (electron density) | 48.24 Å |
| Total Rg | 48.39 Å |
| Atom count | 14725 |
| Residues | 1899 |
| Excluded volume | 261540 ų |
| Maximum q | 0.500 Å⁻¹ |