2SEC
STRUCTURAL COMPARISON OF TWO SERINE PROTEINASE-PROTEIN INHIBITOR COMPLEXES. EGLIN-C-SUBTILISIN CARLSBERG AND CI-2-SUBTILISIN NOVO
Replaces: 1SECEntity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A (E) | SUBTILISIN CARLSBERG | polymer | 274 | 27306.2 | 1 | UniProt (P00780) | Bacillus licheniformis | |
| 2 | B (I) | EGLIN C | polymer | 70 | 8099.0 | 1 | UniProt (P01051) | Hirudo medicinalis (medicinal leech) | |
| 3 | C, D, E (E) | CALCIUM ION | non-polymer | 40.1 | 3 | Chemie (CA) | |||
| 4 | F, G (E, I) | water | water | 18.0 | 170 | Chemie (HOH) |
Sequence modifications
E: 1 - 275 (UniProt: P00780)
I: 15 - 83 (UniProt: P01051)
| PDB | External Database | Details |
|---|---|---|
| Ser 103 | Thr 207 | conflict |
| Ala 129 | Pro 233 | conflict |
| Asn 158 | Ser 262 | conflict |
| Ser 161 | Asn 265 | conflict |
| Asn 212 | Ser 316 | conflict |
| PDB | External Database | Details |
|---|---|---|
| Asn 47 | Asp 33 | conflict |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 2 |
| Total formula weight | 35405.2 | |
| Non-Polymers* | Number of molecules | 3 |
| Total formula weight | 120.2 | |
| All* | Total formula weight | 35525.5 |
