1GHA
A SECOND ACTIVE SITE IN CHYMOTRYPSIN? THE X-RAY CRYSTAL STRUCTURE OF N-ACETYL-D-TRYPTOPHAN BOUND TO GAMMA-CHYMOTRYPSIN
Entity
Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
1 | E | GAMMA-CHYMOTRYPSIN A | polymer | 13 | 1253.5 | 1 | UniProt (P00766) In PDB | Bos taurus (cattle) | |
2 | F | GAMMA-CHYMOTRYPSIN A | polymer | 131 | 13934.6 | 1 | UniProt (P00766) Pfam (PF00089) In PDB | Bos taurus (cattle) | |
3 | G | GAMMA-CHYMOTRYPSIN A | polymer | 97 | 10074.5 | 1 | UniProt (P00766) Pfam (PF00089) In PDB | Bos taurus (cattle) | |
4 | P | PRO GLY VAL TYR PEPTIDE | polymer | 4 | 434.5 | 1 | |||
5 | F | SULFATE ION | non-polymer | 96.1 | 1 | Chemie (SO4) | |||
6 | G | ISOPROPYL ALCOHOL | non-polymer | 60.1 | 1 | Chemie (IPA) | |||
7 | water | water | 18.0 | 173 | Chemie (HOH) |
Sequence viewer
Contents of the asymmetric unit
Polymers | Number of chains | 4 |
Total formula weight | 25697.0 | |
Non-Polymers* | Number of molecules | 2 |
Total formula weight | 156.2 | |
All* | Total formula weight | 25853.2 |