3TNX
Structure of the precursor of a thermostable variant of papain at 2.6 Angstroem resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0006508 | biological_process | proteolysis |
| A | 0008233 | molecular_function | peptidase activity |
| A | 0008234 | molecular_function | cysteine-type peptidase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0097655 | molecular_function | serpin family protein binding |
| C | 0005515 | molecular_function | protein binding |
| C | 0006508 | biological_process | proteolysis |
| C | 0008233 | molecular_function | peptidase activity |
| C | 0008234 | molecular_function | cysteine-type peptidase activity |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0097655 | molecular_function | serpin family protein binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 320 |
| Chain | Residue |
| A | ASN191 |
| A | THR192 |
| A | CYS260 |
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 | Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10088","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"5681232","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6502713","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"952885","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1860874","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1PAD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"9PAP","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10089","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"6502713","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"952885","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1PAD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"9PAP","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10090","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"5681232","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6502713","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"952885","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1PAD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"9PAP","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"covalent","evidences":[{"source":"PubMed","id":"8416808","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1POP","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
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 |
