1ICF
CRYSTAL STRUCTURE OF MHC CLASS II ASSOCIATED P41 II FRAGMENT IN COMPLEX WITH CATHEPSIN L
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 |
Functional Information from PDB Data
| site_id | ACT |
| Number of Residues | 4 |
| Details | ACTIVE SITE |
| Chain | Residue |
| A | CYS25 |
| A | HIS163 |
| C | CYS25 |
| C | HIS163 |
Functional Information from PROSITE/UniProt
| site_id | PS00139 |
| Number of Residues | 12 |
| Details | THIOL_PROTEASE_CYS Eukaryotic thiol (cysteine) proteases cysteine active site. QGqCGSCWAfSA |
| Chain | Residue | Details |
| A | GLN19-ALA30 |
| site_id | PS00484 |
| Number of Residues | 30 |
| Details | THYROGLOBULIN_1_1 Thyroglobulin type-1 repeat signature. FrpkCden.GnYlplQcygsigyc....WCVfpn.G |
| Chain | Residue | Details |
| I | PHE212-GLY241 |
| site_id | PS00639 |
| Number of Residues | 11 |
| Details | THIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. MDHGVLVVGYG |
| Chain | Residue | Details |
| A | MET161-GLY171 |
| site_id | PS00640 |
| Number of Residues | 20 |
| Details | THIOL_PROTEASE_ASN Eukaryotic thiol (cysteine) proteases asparagine active site. YWLvKNSWgeeWGmgGYVkM |
| Chain | Residue | Details |
| B | TYR182-MET201 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"9468501","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 22 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"37990007","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8HFV","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12754519","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 122 |
| Details | Domain: {"description":"Thyroglobulin type-1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00500","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Region: {"description":"Required for interaction with CTSL","evidences":[{"source":"PubMed","id":"10022822","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"32855215","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"10022822","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 8pch |
| Chain | Residue | Details |
| A | GLN19 | |
| A | CYS25 | |
| A | HIS163 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 8pch |
| Chain | Residue | Details |
| C | GLN19 | |
| C | CYS25 | |
| C | HIS163 |
