3E1Z
Crystal structure of the parasite protesase inhibitor chagasin in complex with papain
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004869 | molecular_function | cysteine-type endopeptidase inhibitor activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0009986 | cellular_component | cell surface |
| A | 0020016 | cellular_component | ciliary pocket |
| A | 0030414 | molecular_function | peptidase inhibitor activity |
| A | 0031410 | cellular_component | cytoplasmic vesicle |
| B | 0006508 | biological_process | proteolysis |
| B | 0008234 | molecular_function | cysteine-type peptidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 111 |
| Chain | Residue |
| A | GLU23 |
| A | HIS72 |
| A | HIS74 |
| A | FMT113 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE FMT A 112 |
| Chain | Residue |
| B | GLY101 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FMT A 113 |
| Chain | Residue |
| A | ZN111 |
| A | HOH141 |
| B | TYR61 |
| A | GLU23 |
| A | PHE58 |
| A | HIS72 |
| A | HIS74 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT A 114 |
| Chain | Residue |
| A | PHE34 |
| A | SER97 |
| A | HIS98 |
| A | ASP99 |
| A | HOH148 |
| B | ASN18 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ACY B 213 |
| Chain | Residue |
| A | ASN29 |
| A | THR31 |
| A | THR32 |
| A | GLY66 |
| B | GLN19 |
| B | GLY23 |
| B | SER24 |
| B | CYS25 |
| B | ASP158 |
| B | HIS159 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FMT B 214 |
| Chain | Residue |
| B | SER124 |
| B | ASN127 |
| B | GLN128 |
| B | TYR208 |
| B | HOH380 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE FMT B 215 |
| Chain | Residue |
| B | TYR78 |
| B | HIS81 |
| B | HOH382 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE FMT B 216 |
| Chain | Residue |
| B | ARG98 |
| B | HOH382 |
| site_id | AC9 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE FMT B 217 |
| Chain | Residue |
| B | HOH400 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE FMT B 218 |
| Chain | Residue |
| A | GLU20 |
| B | GLN92 |
| B | HOH390 |
| site_id | BC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE FMT B 219 |
| Chain | Residue |
| B | LYS190 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FMT B 220 |
| Chain | Residue |
| B | GLN9 |
| B | ILE40 |
| B | HOH298 |
| B | HOH400 |
| B | HOH441 |
Functional Information from PROSITE/UniProt
| site_id | PS00139 |
| Number of Residues | 12 |
| Details | THIOL_PROTEASE_CYS Eukaryotic thiol (cysteine) proteases cysteine active site. QGsCGSCWAfSA |
| Chain | Residue | Details |
| B | GLN19-ALA30 |
| site_id | PS00639 |
| Number of Residues | 11 |
| Details | THIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. VDHAVAAVGYG |
| Chain | Residue | Details |
| B | VAL157-GLY167 |
| site_id | PS00640 |
| Number of Residues | 20 |
| Details | THIOL_PROTEASE_ASN Eukaryotic thiol (cysteine) proteases asparagine active site. YILiKNSWgtgWGenGYIrI |
| Chain | Residue | Details |
| B | TYR170-ILE189 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 5 |
| Details | Motif: {"description":"BC loop","evidences":[{"source":"PubMed","id":"17502099","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17561110","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18515357","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19143838","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 9 |
| Details | Motif: {"description":"DE loop","evidences":[{"source":"PubMed","id":"17502099","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17561110","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18515357","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19143838","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 9 |
| Details | Motif: {"description":"FG loop","evidences":[{"source":"PubMed","id":"17502099","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17561110","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18515357","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19143838","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| 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_FI5 |
| Number of Residues | 1 |
| 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_FI6 |
| Number of Residues | 1 |
| 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_FI7 |
| Number of Residues | 1 |
| 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 | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1pad |
| Chain | Residue | Details |
| B | ASN175 | |
| B | CYS25 | |
| B | HIS159 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1pad |
| Chain | Residue | Details |
| B | GLN19 | |
| B | CYS25 | |
| B | HIS159 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1pad |
| Chain | Residue | Details |
| B | ASN175 | |
| B | GLN19 | |
| B | HIS159 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 174 |
| Chain | Residue | Details |
| B | GLN19 | electrostatic stabiliser, hydrogen bond donor |
| B | CYS25 | electrostatic stabiliser |
| B | HIS159 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | ASN175 | activator, electrostatic stabiliser, hydrogen bond acceptor |
