2DQA
Crystal Structure of Tapes japonica Lysozyme
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003796 | molecular_function | lysozyme activity |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004568 | molecular_function | chitinase activity |
| A | 0005576 | cellular_component | extracellular region |
| A | 0008233 | molecular_function | peptidase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0031640 | biological_process | killing of cells of another organism |
| A | 0042742 | biological_process | defense response to bacterium |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0061929 | molecular_function | gamma-glutamylaminecyclotransferase activity |
| B | 0003796 | molecular_function | lysozyme activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004568 | molecular_function | chitinase activity |
| B | 0005576 | cellular_component | extracellular region |
| B | 0008233 | molecular_function | peptidase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0031640 | biological_process | killing of cells of another organism |
| B | 0042742 | biological_process | defense response to bacterium |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0061929 | molecular_function | gamma-glutamylaminecyclotransferase activity |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 232 |
| Details | Domain: {"description":"I-type lysozyme","evidences":[{"source":"PROSITE-ProRule","id":"PRU01257","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01257","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17631496","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU01257","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17631496","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 22 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17631496","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2DQA","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
