2CJX
Extended substrate recognition in caspase-3 revealed by high resolution X-ray structure analysis
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A (A) | CASPASE-3 | polymer | 147 | 16639.9 | 1 | UniProt (P42574) Pfam (PF00656) | HOMO SAPIENS (HUMAN) | CASP-3, APOPAIN, CYSTEINE PROTEASE CPP32, CPP-32, PROTEIN YAMA, SREBP CLEAVAGE ACTIVITY 1, SCA-1, CASPASE-3 SUBUNIT P17, CASPASE-3 SUBUNIT P12 |
| 2 | B (B) | CASPASE-3 | polymer | 103 | 11937.7 | 1 | UniProt (P42574) Pfam (PF00656) | HOMO SAPIENS (HUMAN) | CASP-3, APOPAIN, CYSTEINE PROTEASE CPP32, CPP-32, PROTEIN YAMA, SREBP CLEAVAGE ACTIVITY 1, SCA-1, CASPASE-3 SUBUNIT P17, CASPASE-3 SUBUNIT P12 |
| 3 | C (I) | PHQ-ASP-GLU-VAL-ASP-CHLOROMETHYLKETONE | polymer | 6 | 661.5 | 1 | BIRD (PRD_000277) | SYNTHETIC CONSTRUCT | Z-DEVD-CMK |
| 4 | D, E, F (A, B, I) | water | water | 18.0 | 372 | Chemie (HOH) |
Sequence modifications
B: 176 - 277 (UniProt: P42574)
| PDB | External Database | Details |
|---|---|---|
| Ala 175 | - | cloning artifact |
| Ala 179 | Asp 179 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 3 |
| Total formula weight | 29239.1 | |
| All* | Total formula weight | 29239.1 |
