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 | RHIZOPUSPEPSIN | polymer | 325 | 34068.6 | 1 | UniProt (P06026) Pfam (PF00026) In PDB | Rhizopus microsporus var. chinensis | |
2 | A | CALCIUM ION | non-polymer | 40.1 | 1 | Chemie (CA) | |||
3 | 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 |