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 | CSDE1_HUMAN |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 8–83； UniProt 15–90 |
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 | 1wfq |
| Deposition date deposition_date | 2004-05-26 |
| Structure title title | Solution structure of the first cold-shock domain of the human KIAA0885 protein (UNR protein) |
| Keywords keywords | ;Beta-barrel, translational regulation, RNA chaperone, RNA/DNA binding, QB fold, Greek-key topology, unr protein, structural genomics, RIKEN Structural Genomics/Proteomics Initiative, RSGI, RNA BINDING PROTEIN ;; RNA BINDING PROTEIN |
| 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） | 15.56 Å |
| Rg (electron density) | 14.02 Å |
| Total Rg | 15.31 Å |
| Atom count | 1316 |
| Residues | 89 |
| Excluded volume | 11660 ų |
| Maximum q | 0.500 Å⁻¹ |
| Assembly | Model | Structure unit | Oligomeric description | Status | CRYSOL | Actions |
|---|---|---|---|---|---|---|
| 1 | 1 | 1wfq__assembly_1__model_1 |
monomeric （1） | Success | 4.1.3-1-20251215 (887e7ef) | View Download |
| 1 | 2 | 1wfq__assembly_1__model_2 |
monomeric （1） | Success | 4.1.3-1-20251215 (887e7ef) | View Download |
| 1 | 3 | 1wfq__assembly_1__model_3 |
monomeric （1） | Success | 4.1.3-1-20251215 (887e7ef) | View Download |
| 1 | 4 | 1wfq__assembly_1__model_4 |
monomeric （1） | Success | 4.1.3-1-20251215 (887e7ef) | View Download |
| 1 | 5 | 1wfq__assembly_1__model_5 |
monomeric （1） | Success | 4.1.3-1-20251215 (887e7ef) | View Download |
| 1 | 6 | 1wfq__assembly_1__model_6 |
monomeric （1） | Success | 4.1.3-1-20251215 (887e7ef) | View Download |
| 1 | 7 | 1wfq__assembly_1__model_7 |
monomeric （1） | Success | 4.1.3-1-20251215 (887e7ef) | View Download |
| 1 | 8 | 1wfq__assembly_1__model_8 |
monomeric （1） | Success | 4.1.3-1-20251215 (887e7ef) | View Download |
| 1 | 9 | 1wfq__assembly_1__model_9 |
monomeric （1） | Success | 4.1.3-1-20251215 (887e7ef) | View Download |
| 1 | 10 | 1wfq__assembly_1__model_10 |
monomeric （1） | Success | 4.1.3-1-20251215 (887e7ef) | View Download |
| 1 | 11 | 1wfq__assembly_1__model_11 |
monomeric （1） | Success | 4.1.3-1-20251215 (887e7ef) | View Download |
| 1 | 12 | 1wfq__assembly_1__model_12 |
monomeric （1） | Success | 4.1.3-1-20251215 (887e7ef) | View Download |
| 1 | 13 | 1wfq__assembly_1__model_13 |
monomeric （1） | Success | 4.1.3-1-20251215 (887e7ef) | View Download |
| 1 | 14 | 1wfq__assembly_1__model_14 |
monomeric （1） | Success | 4.1.3-1-20251215 (887e7ef) | View Download |
| 1 | 15 | 1wfq__assembly_1__model_15 |
monomeric （1） | Success | 4.1.3-1-20251215 (887e7ef) | View Download |
| 1 | 16 | 1wfq__assembly_1__model_16 |
monomeric （1） | Success | 4.1.3-1-20251215 (887e7ef) | View Download |
| 1 | 17 | 1wfq__assembly_1__model_17 |
monomeric （1） | Success | 4.1.3-1-20251215 (887e7ef) | View Download |
| 1 | 18 | 1wfq__assembly_1__model_18 |
monomeric （1） | Success | 4.1.3-1-20251215 (887e7ef) | View Download |
| 1 | 19 | 1wfq__assembly_1__model_19 |
monomeric （1） | Success | 4.1.3-1-20251215 (887e7ef) | View Download |
| 1 | 20 | 1wfq__assembly_1__model_20 |
monomeric （1） | Success | 4.1.3-1-20251215 (887e7ef) | View Download |
| Domain ID domain_id | d1wfqa1 |
| Class class | b — All beta proteins |
| Fold Fold fold | b.40 — OB-fold |
| Superfamily Superfamily superfamily | b.40.4 — Nucleic acid-binding proteins |
| Family Family family | b.40.4.5 — Cold shock DNA-binding domain-like |
| Domain ID domain_id | d1wfqa2 |
| 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 | d1wfqa3 |
| 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 | 1wfqA01 |
| Class class | 2 — Mainly Beta |
| Architecture architecture | 40 — Beta Barrel |
| Topology topology | 50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P) |
| Homologous superfamily homologous superfamily | 140 — Nucleic acid-binding proteins |