4I04
Structure of zymogen of cathepsin B1 from Schistosoma mansoni
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004197 | molecular_function | cysteine-type endopeptidase activity |
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 | 0050790 | biological_process | regulation of catalytic activity |
B | 0004197 | molecular_function | cysteine-type endopeptidase activity |
B | 0006508 | biological_process | proteolysis |
B | 0008233 | molecular_function | peptidase activity |
B | 0008234 | molecular_function | cysteine-type peptidase activity |
B | 0016787 | molecular_function | hydrolase activity |
B | 0050790 | biological_process | regulation of catalytic activity |
C | 0004197 | molecular_function | cysteine-type endopeptidase activity |
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 | 0050790 | biological_process | regulation of catalytic activity |
D | 0004197 | molecular_function | cysteine-type endopeptidase activity |
D | 0006508 | biological_process | proteolysis |
D | 0008233 | molecular_function | peptidase activity |
D | 0008234 | molecular_function | cysteine-type peptidase activity |
D | 0016787 | molecular_function | hydrolase activity |
D | 0050790 | biological_process | regulation of catalytic activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 401 |
Chain | Residue |
A | PHE76 |
A | ASP77 |
A | LYS80 |
A | LYS81 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO A 402 |
Chain | Residue |
C | ASN281 |
C | LYS282 |
A | VAL279 |
A | ASN281 |
A | LYS282 |
C | VAL279 |
C | GLU280 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO B 401 |
Chain | Residue |
B | ARG79 |
B | TRP82 |
B | CYS85 |
B | LYS86 |
B | ILE88 |
B | ALA89 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B 402 |
Chain | Residue |
B | ALA89 |
B | THR90 |
B | ILE91 |
B | GLU294 |
B | HOH548 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B 403 |
Chain | Residue |
B | PHE76 |
B | ASP77 |
B | LYS81 |
B | HOH579 |
B | HOH637 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO D 401 |
Chain | Residue |
B | VAL279 |
B | ASN281 |
B | LYS282 |
D | VAL279 |
D | ASN281 |
D | LYS282 |
D | HOH592 |
Functional Information from PROSITE/UniProt
site_id | PS00639 |
Number of Residues | 11 |
Details | THIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. GGHAIRIIGWG |
Chain | Residue | Details |
A | GLY268-GLY278 |
site_id | PS00640 |
Number of Residues | 20 |
Details | THIOL_PROTEASE_ASN Eukaryotic thiol (cysteine) proteases asparagine active site. YWLiANSWnedWGenGYFrI |
Chain | Residue | Details |
A | TYR285-ILE304 |