Thermotoga maritima
| 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 | Q9X298_THEMA |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–369； UniProt 1–344 |
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 | 1l2f |
| Deposition date deposition_date | 2002-02-20 |
| Structure title title | Crystal structure of NusA from Thermotoga maritima: a structure-based role of the N-terminal domain |
| Keywords keywords | ;NusA, OB fold KH domain, RNA polymerase, Structural Genomics, BSGC structure funded by NIH, Protein Structure Initiative, PSI, Berkeley Structural Genomics Center, TRANSCRIPTION ;; TRANSCRIPTION |
| 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） | 34.31 Å |
| Rg (electron density) | 34.88 Å |
| Total Rg | 34.94 Å |
| Atom count | 2667 |
| Residues | 340 |
| Excluded volume | 48539 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d1l2fa1 |
| 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 | d1l2fa2 |
| Class class | d — Alpha and beta proteins (a+b) |
| Fold Fold fold | d.52 — Alpha-lytic protease prodomain-like |
| Superfamily Superfamily superfamily | d.52.3 — Prokaryotic type KH domain (KH-domain type II) |
| Family Family family | d.52.3.1 — Prokaryotic type KH domain (KH-domain type II) |
| Domain ID domain_id | d1l2fa3 |
| Class class | d — Alpha and beta proteins (a+b) |
| Fold Fold fold | d.52 — Alpha-lytic protease prodomain-like |
| Superfamily Superfamily superfamily | d.52.3 — Prokaryotic type KH domain (KH-domain type II) |
| Family Family family | d.52.3.1 — Prokaryotic type KH domain (KH-domain type II) |
| Domain ID domain_id | d1l2fa4 |
| Class class | d — Alpha and beta proteins (a+b) |
| Fold Fold fold | d.202 — Transcription factor NusA, N-terminal domain |
| Superfamily Superfamily superfamily | d.202.1 — Transcription factor NusA, N-terminal domain |
| Family Family family | d.202.1.1 — Transcription factor NusA, N-terminal domain |
| Domain ID domain_id | 1l2fA01 |
| Class class | 3 — Alpha Beta |
| Architecture architecture | 30 — 2-Layer Sandwich |
| Topology topology | 1480 — N Utilization Substance Protein A; Chain:P; domain 4 |
| Homologous superfamily homologous superfamily | 10 — NusA, N-terminal domain |
| Domain ID domain_id | 1l2fA02 |
| 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 |
| Domain ID domain_id | 1l2fA03 |
| Class class | 3 — Alpha Beta |
| Architecture architecture | 30 — 2-Layer Sandwich |
| Topology topology | 300 — GMP Synthetase; Chain A, domain 3 |
| Homologous superfamily homologous superfamily | 20 — K homology (KH) domain |
| Domain ID domain_id | 1l2fA04 |
| Class class | 3 — Alpha Beta |
| Architecture architecture | 30 — 2-Layer Sandwich |
| Topology topology | 300 — GMP Synthetase; Chain A, domain 3 |
| Homologous superfamily homologous superfamily | 20 — K homology (KH) domain |