Rattus norvegicus
| Assembly | Physical composition | Protein state | Molecular copy count | Associated components | Data consistency |
|---|---|---|---|---|---|
| 1 | Protein monomer | Monomer | Protein 1 | MYRISTIC ACID × 1 water × 1 | Consistent with protein count |
| UniProt name | FABPI_RAT |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–131； UniProt 1–131 |
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 | 1icm |
| Deposition date deposition_date | 1993-09-20 |
| Structure title title | ESCHERICHIA COLI-DERIVED RAT INTESTINAL FATTY ACID BINDING PROTEIN WITH BOUND MYRISTATE AT 1.5 A RESOLUTION AND I-FABPARG106-->GLN WITH BOUND OLEATE AT 1.74 A RESOLUTION |
| Keywords keywords | BINDING PROTEIN(FATTY ACID); BINDING PROTEIN(FATTY ACID) |
| 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） | 15.61 Å |
| Rg (electron density) | 14.10 Å |
| Total Rg | 15.46 Å |
| Atom count | 1073 |
| Residues | 131 |
| Excluded volume | 19226 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d1icma_ |
| Class class | b — All beta proteins |
| Fold Fold fold | b.60 — Lipocalins |
| Superfamily Superfamily superfamily | b.60.1 — Lipocalins |
| Family Family family | b.60.1.2 — Fatty acid binding protein-like |
| Domain ID domain_id | 1icmA00 |
| Class class | 2 — Mainly Beta |
| Architecture architecture | 40 — Beta Barrel |
| Topology topology | 128 — Lipocalin |
| Homologous superfamily homologous superfamily | 20 — Calycin beta-barrel core domain |