4PJ2
Crystal structure of Aeromonas hydrophila PliI in complex with Meretrix lusoria lysozyme
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0003796 | molecular_function | lysozyme activity |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004568 | molecular_function | chitinase activity |
| C | 0005576 | cellular_component | extracellular region |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| C | 0031640 | biological_process | killing of cells of another organism |
| C | 0042742 | biological_process | defense response to bacterium |
| D | 0003796 | molecular_function | lysozyme activity |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004568 | molecular_function | chitinase activity |
| D | 0005576 | cellular_component | extracellular region |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| D | 0031640 | biological_process | killing of cells of another organism |
| D | 0042742 | biological_process | defense response to bacterium |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | binding site for residue GOL A 201 |
| Chain | Residue |
| A | SER38 |
| B | ASP51 |
| B | ARG53 |
| A | ARG41 |
| A | ASP51 |
| A | ARG53 |
| A | HOH348 |
| A | HOH355 |
| A | HOH415 |
| B | SER38 |
| B | ARG41 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 202 |
| Chain | Residue |
| A | ASP65 |
| A | GLN66 |
| A | HOH352 |
| A | HOH434 |
| B | THR47 |
| C | TYR76 |
| C | TRP79 |
| C | ALA80 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 203 |
| Chain | Residue |
| A | ASP86 |
| A | ASN88 |
| A | ASP90 |
| A | GLN92 |
| A | GLU94 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue MG B 201 |
| Chain | Residue |
| B | LEU29 |
| B | PRO30 |
| B | SER31 |
| B | LYS91 |
| B | GLN92 |
| B | PRO93 |
| B | HOH301 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI2 |
| Number of Residues | 230 |
| Details | Domain: {"description":"I-type lysozyme","evidences":[{"source":"PROSITE-ProRule","id":"PRU01257","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01257","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU01257","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"24192349","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"MAY-2011","submissionDatabase":"PDB data bank","title":"Crystal structure of inhibitor bound lysozyme from Meretrix lusoria.","authors":["Yoneda K.","Kuwano Y.","Usui T.","Ogata M.","Suzuki A.","Araki T."]}},{"source":"PDB","id":"3AB6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3AYQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q8IU26","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
