OrganismNot specified
| 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 | MCPI_HIRME |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–67； UniProt 15–81 |
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 | 1dtv |
| Deposition date deposition_date | 2000-01-13 |
| Structure title title | NMR STRUCTURE OF THE LEECH CARBOXYPEPTIDASE INHIBITOR (LCI) |
| Keywords keywords | Leech Carboxypeptidase Inhibitor, LCI, HYDROLASE INHIBITOR; HYDROLASE INHIBITOR |
| 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） | 12.61 Å |
| Rg (electron density) | 11.60 Å |
| Total Rg | 12.65 Å |
| Atom count | 974 |
| Residues | 67 |
| Excluded volume | 8972 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d1dtva_ |
| Class class | g — Small proteins |
| Fold Fold fold | g.30 — Carboxypeptidase inhibitor |
| Superfamily Superfamily superfamily | g.30.1 — Carboxypeptidase inhibitor |
| Family Family family | g.30.1.1 — Carboxypeptidase inhibitor |
| Domain ID domain_id | 1dtvA00 |
| Class class | 3 — Alpha Beta |
| Architecture architecture | 30 — 2-Layer Sandwich |
| Topology topology | 1040 — Carboxypeptidase Inhibitor; Chain A |
| Homologous superfamily homologous superfamily | 10 — Carboxypeptidase inhibitor |