2APR
STRUCTURE AND REFINEMENT AT 1.8 ANGSTROMS RESOLUTION OF THE ASPARTIC PROTEINASE FROM RHIZOPUS CHINENSIS
Replaces: 1APREntity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A (A) | RHIZOPUSPEPSIN | polymer | 325 | 34068.6 | 1 | UniProt (P06026) Pfam (PF00026) | Rhizopus microsporus var. chinensis | |
| 2 | B (A) | CALCIUM ION | non-polymer | 40.1 | 1 | Chemie (CA) | |||
| 3 | C (A) | water | water | 18.0 | 373 | Chemie (HOH) |
Sequence modifications
A: 1 - 324 (UniProt: P06026)
| PDB | External Database | Details |
|---|---|---|
| Ile 15 | Val 83 | conflict |
| Gly 54 | Arg 122 | conflict |
| Asn 61 | Lys 129 | conflict |
| Ser 116 | Asn 184 | conflict |
| Lys 162 | Ser 230 | conflict |
| Ile 230 | Val 298 | conflict |
| Ala 256 | Arg 324 | conflict |
| Phe 281 | Tyr 349 | conflict |
| Trp 294 | Phe 362 | conflict |
| Gly 295 | Asp 363 | conflict |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 1 |
| Total formula weight | 34068.6 | |
| Non-Polymers* | Number of molecules | 1 |
| Total formula weight | 40.1 | |
| All* | Total formula weight | 34108.7 |
