1u9g
Heterocyclic Peptide Backbone Modification in GCN4-pLI Based Coiled Coils: Replacement of K(8)L(9)
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 | 4 / 0 / 0 / 0 | Consistent with protein count |
| 2 | Protein homooligomer | Homooligomer | 6 / 0 / 0 / 0 | Consistent with protein count |
| 3 | Protein homooligomer | Homooligomer | 6 / 0 / 0 / 0 | Consistent with protein count |
| 4 | Protein homooligomer | Homooligomer | 6 / 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 | 1u9g |
| Deposition date deposition_date | 2004-08-09 |
| Structure title title | Heterocyclic Peptide Backbone Modification in GCN4-pLI Based Coiled Coils: Replacement of K(8)L(9) |
| Keywords keywords | tetrameric alpha-helical coiled coil with heteerocycic backbone modification, transcription; TRANSCRIPTION |
| 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.
1u9g__assembly_1__model_1
Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)
1u9g__assembly_1__model_1 | I(q)
1u9g__assembly_1__model_1 | P(r) · Pending
| Rg（Guinier） | 14.00 Å |
| Rg (electron density) | 12.50 Å |
| Total Rg | 13.82 Å |
| Atom count | 736 |
| Residues | 84 |
| Excluded volume | 13246 ų |
| Maximum q | 0.500 Å⁻¹ |
| Assembly | Model | Structure unit | Oligomeric description | Status | CRYSOL | Actions |
|---|---|---|---|---|---|---|
| 1 | 1 | 1u9g__assembly_1__model_1 |
tetrameric （4） | Success | 4.1.3-1-20251215 (887e7ef) | View Download |
| 2 | 1 | 1u9g__assembly_2__model_1 |
hexameric （6） | Success | 4.1.3-1-20251215 (887e7ef) | View Download |
| 3 | 1 | 1u9g__assembly_3__model_1 |
hexameric （6） | Success | 4.1.3-1-20251215 (887e7ef) | View Download |
| 4 | 1 | 1u9g__assembly_4__model_1 |
hexameric （6） | Success | 4.1.3-1-20251215 (887e7ef) | View Download |
4. Crystallography and Experiment 4. Crystallography & Experiment
5. Entities and Polymers Entities & Polymers (3)
6. Fold Classification (SCOP + CATH) 2 domains
SCOP 2.08 (2 domains)
| Domain ID domain_id | d1u9ga_ |
| Class class | h — Coiled coil proteins |
| Fold Fold fold | h.1 — Parallel coiled-coil |
| Superfamily Superfamily superfamily | h.1.3 — Leucine zipper domain |
| Family Family family | h.1.3.1 — Leucine zipper domain |
| Domain ID domain_id | d1u9gb_ |
| Class class | h — Coiled coil proteins |
| Fold Fold fold | h.1 — Parallel coiled-coil |
| Superfamily Superfamily superfamily | h.1.3 — Leucine zipper domain |
| Family Family family | h.1.3.1 — Leucine zipper domain |