3H6S
Structure of clitocypin - cathepsin V complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006508 | biological_process | proteolysis |
| A | 0008234 | molecular_function | cysteine-type peptidase activity |
| B | 0006508 | biological_process | proteolysis |
| B | 0008234 | molecular_function | cysteine-type peptidase activity |
| C | 0006508 | biological_process | proteolysis |
| C | 0008234 | molecular_function | cysteine-type peptidase activity |
| D | 0006508 | biological_process | proteolysis |
| D | 0008234 | molecular_function | cysteine-type peptidase activity |
| E | 0004869 | molecular_function | cysteine-type endopeptidase inhibitor activity |
| E | 0030414 | molecular_function | peptidase inhibitor activity |
| F | 0004869 | molecular_function | cysteine-type endopeptidase inhibitor activity |
| F | 0030414 | molecular_function | peptidase inhibitor activity |
| G | 0004869 | molecular_function | cysteine-type endopeptidase inhibitor activity |
| G | 0030414 | molecular_function | peptidase inhibitor activity |
| H | 0004869 | molecular_function | cysteine-type endopeptidase inhibitor activity |
| H | 0030414 | molecular_function | peptidase inhibitor activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 222 |
| Chain | Residue |
| A | GLY118 |
| A | LYS119 |
| A | GLU120 |
| A | LYS121 |
| A | HOH383 |
| A | HOH700 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 B 222 |
| Chain | Residue |
| B | LYS201 |
| B | HOH614 |
| B | HOH762 |
| B | HOH830 |
| C | LEU1 |
| B | SER149 |
| B | GLY150 |
| B | SER196 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 223 |
| Chain | Residue |
| B | GLY118 |
| B | LYS119 |
| B | GLU120 |
| B | LYS121 |
| B | HOH348 |
| B | HOH371 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 C 222 |
| Chain | Residue |
| C | GLY118 |
| C | LYS119 |
| C | GLU120 |
| C | LYS121 |
| C | HOH224 |
| C | HOH341 |
| C | HOH393 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 D 222 |
| Chain | Residue |
| D | GLY118 |
| D | LYS119 |
| D | GLU120 |
| D | LYS121 |
| D | HOH470 |
| D | HOH815 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 F 153 |
| Chain | Residue |
| F | ARG34 |
| F | GLY91 |
| F | ASP92 |
| F | LYS94 |
| F | HOH472 |
| F | HOH853 |
Functional Information from PROSITE/UniProt
| site_id | PS00139 |
| Number of Residues | 12 |
| Details | THIOL_PROTEASE_CYS Eukaryotic thiol (cysteine) proteases cysteine active site. QKqCGSCWAfSA |
| Chain | Residue | Details |
| A | GLN19-ALA30 |
| site_id | PS00639 |
| Number of Residues | 11 |
| Details | THIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. LDHGVLVVGYG |
| Chain | Residue | Details |
| A | LEU162-GLY172 |
| site_id | PS00640 |
| Number of Residues | 20 |
| Details | THIOL_PROTEASE_ASN Eukaryotic thiol (cysteine) proteases asparagine active site. YWLvKNSWgpeWGsnGYVkI |
| Chain | Residue | Details |
| A | TYR183-ILE202 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"11027133","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"22967898","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1pad |
| Chain | Residue | Details |
| A | HIS164 | |
| A | ASN188 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1pad |
| Chain | Residue | Details |
| B | HIS164 | |
| B | ASN188 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1pad |
| Chain | Residue | Details |
| C | HIS164 | |
| C | ASN188 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1pad |
| Chain | Residue | Details |
| D | HIS164 | |
| D | ASN188 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1pad |
| Chain | Residue | Details |
| A | HIS164 | |
| A | GLN19 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1pad |
| Chain | Residue | Details |
| B | HIS164 | |
| B | GLN19 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1pad |
| Chain | Residue | Details |
| C | HIS164 | |
| C | GLN19 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1pad |
| Chain | Residue | Details |
| D | HIS164 | |
| D | GLN19 |
| site_id | CSA9 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1pad |
| Chain | Residue | Details |
| A | HIS164 | |
| A | GLN19 | |
| A | ASN188 |
| site_id | CSA10 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1pad |
| Chain | Residue | Details |
| B | HIS164 | |
| B | GLN19 | |
| B | ASN188 |
| site_id | CSA11 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1pad |
| Chain | Residue | Details |
| C | HIS164 | |
| C | GLN19 | |
| C | ASN188 |
| site_id | CSA12 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1pad |
| Chain | Residue | Details |
| D | HIS164 | |
| D | GLN19 | |
| D | ASN188 |
