4QRX
Crystal structure of pro-papain mutant at pH 4.0
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004197 | molecular_function | cysteine-type endopeptidase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005764 | cellular_component | lysosome |
| A | 0006508 | biological_process | proteolysis |
| A | 0008234 | molecular_function | cysteine-type peptidase activity |
| A | 0051603 | biological_process | proteolysis involved in protein catabolic process |
| A | 0097655 | molecular_function | serpin family protein binding |
| C | 0004197 | molecular_function | cysteine-type endopeptidase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005615 | cellular_component | extracellular space |
| C | 0005764 | cellular_component | lysosome |
| C | 0006508 | biological_process | proteolysis |
| C | 0008234 | molecular_function | cysteine-type peptidase activity |
| C | 0051603 | biological_process | proteolysis involved in protein catabolic process |
| C | 0097655 | molecular_function | serpin family protein binding |
Functional Information from PROSITE/UniProt
| site_id | PS00639 |
| Number of Residues | 11 |
| Details | THIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. VDHAVAAVGYG |
| Chain | Residue | Details |
| A | VAL264-GLY274 |
| site_id | PS00640 |
| Number of Residues | 20 |
| Details | THIOL_PROTEASE_ASN Eukaryotic thiol (cysteine) proteases asparagine active site. YILiRNSWgtgWGenGYIrI |
| Chain | Residue | Details |
| A | TYR277-ILE296 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10088, ECO:0000269|PubMed:5681232, ECO:0000269|PubMed:6502713, ECO:0000269|PubMed:952885, ECO:0000305|PubMed:1860874, ECO:0007744|PDB:1PAD, ECO:0007744|PDB:9PAP |
| Chain | Residue | Details |
| A | ALA132 | |
| C | ALA132 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10089, ECO:0000269|PubMed:6502713, ECO:0000269|PubMed:952885, ECO:0007744|PDB:1PAD, ECO:0007744|PDB:9PAP |
| Chain | Residue | Details |
| A | HIS266 | |
| C | HIS266 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10090, ECO:0000269|PubMed:5681232, ECO:0000269|PubMed:6502713, ECO:0000269|PubMed:952885, ECO:0007744|PDB:1PAD, ECO:0007744|PDB:9PAP |
| Chain | Residue | Details |
| A | ASN282 | |
| C | ASN282 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: covalent => ECO:0000269|PubMed:8416808, ECO:0007744|PDB:1POP |
| Chain | Residue | Details |
| A | ALA132 | |
| C | ALA132 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 174 |
| Chain | Residue | Details |
| A | GLN126 | electrostatic stabiliser, hydrogen bond donor |
| A | ALA132 | electrostatic stabiliser |
| A | HIS266 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | ASN282 | activator, electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 174 |
| Chain | Residue | Details |
| C | GLN126 | electrostatic stabiliser, hydrogen bond donor |
| C | ALA132 | electrostatic stabiliser |
| C | HIS266 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| C | ASN282 | activator, electrostatic stabiliser, hydrogen bond acceptor |
