2gqw
Crystal structure of Ferredoxin reductase, BphA4 (oxidized form)
1. Protein Identity and Related Structures Protein Identity & Related Structures
No usable UniProt protein identity is available for this entry.
The relationship tables retain this entry's assembly and composition data, but cross-PDB links for the same protein cannot be established reliably without a unified protein identity.
Assembly Composition of the Current Entry
| Assembly | Physical composition | Protein state | 蛋白 / DNA / RNA / 其他Polymer | Data consistency |
|---|---|---|---|---|
| 1 | Protein homooligomer | Homooligomer | 2 / 0 / 0 / 0 | Consistent with protein count |
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.
2. Structure Basics 2. Structure Basics
| Entry ID entry_id | 2gqw |
| Deposition date deposition_date | 2006-04-22 |
| Structure title title | Crystal structure of Ferredoxin reductase, BphA4 (oxidized form) |
| Keywords keywords | Flavoprotein, OXIDOREDUCTASE; OXIDOREDUCTASE |
| Experimental Method method | X-RAY DIFFRACTION |
3. Official assembly/model SAXS Official SAXS Profiles
This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.
2gqw__assembly_1__model_1
Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)
2gqw__assembly_1__model_1 | I(q)
2gqw__assembly_1__model_1 | P(r) · Pending
| Rg（Guinier） | 30.24 Å |
| Rg (electron density) | 29.26 Å |
| Total Rg | 30.05 Å |
| Atom count | 6090 |
| Residues | 802 |
| Excluded volume | 107810 ų |
| Maximum q | 0.500 Å⁻¹ |
4. Crystallography and Experiment 4. Crystallography & Experiment
5. Entities and Polymers Entities & Polymers (5)
6. Fold Classification (SCOP + CATH) 7 domains
SCOP 2.08 (4 domains)
| Domain ID domain_id | d2gqwa1 |
| Class class | c — Alpha and beta proteins (a/b) |
| Fold Fold fold | c.3 — FAD/NAD(P)-binding domain |
| Superfamily Superfamily superfamily | c.3.1 — FAD/NAD(P)-binding domain |
| Family Family family | c.3.1.5 — FAD/NAD-linked reductases, N-terminal and central domains |
| Domain ID domain_id | d2gqwa2 |
| Class class | c — Alpha and beta proteins (a/b) |
| Fold Fold fold | c.3 — FAD/NAD(P)-binding domain |
| Superfamily Superfamily superfamily | c.3.1 — FAD/NAD(P)-binding domain |
| Family Family family | c.3.1.5 — FAD/NAD-linked reductases, N-terminal and central domains |
| Domain ID domain_id | d2gqwa3 |
| Class class | d — Alpha and beta proteins (a+b) |
| Fold Fold fold | d.87 — CO dehydrogenase flavoprotein C-domain-like |
| Superfamily Superfamily superfamily | d.87.1 — FAD/NAD-linked reductases, dimerisation (C-terminal) domain |
| Family Family family | d.87.1.1 — FAD/NAD-linked reductases, dimerisation (C-terminal) domain |
| Domain ID domain_id | d2gqwa4 |
| 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 |
CATH v4.4 (3 domains)
| Domain ID domain_id | 2gqwA01 |
| Class class | 3 — Alpha Beta |
| Architecture architecture | 50 — 3-Layer(bba) Sandwich |
| Topology topology | 50 — FAD/NAD(P)-binding domain |
| Homologous superfamily homologous superfamily | 60 — FAD/NAD(P)-binding domain |
| Domain ID domain_id | 2gqwA02 |
| Class class | 3 — Alpha Beta |
| Architecture architecture | 50 — 3-Layer(bba) Sandwich |
| Topology topology | 50 — FAD/NAD(P)-binding domain |
| Homologous superfamily homologous superfamily | 60 — FAD/NAD(P)-binding domain |
| Domain ID domain_id | 2gqwA03 |
| Class class | 3 — Alpha Beta |
| Architecture architecture | 30 — 2-Layer Sandwich |
| Topology topology | 390 — Enolase-like; domain 1 |
| Homologous superfamily homologous superfamily | 30 — FAD/NAD-linked reductase, C-terminal dimerisation domain |