1WTH
Crystal structure of gp5-S351L mutant and gp27 complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003796 | molecular_function | lysozyme activity |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0009253 | biological_process | peptidoglycan catabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0016998 | biological_process | cell wall macromolecule catabolic process |
| A | 0031640 | biological_process | killing of cells of another organism |
| A | 0042742 | biological_process | defense response to bacterium |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0044409 | biological_process | symbiont entry into host |
| A | 0044423 | cellular_component | virion component |
| A | 0046718 | biological_process | symbiont entry into host cell |
| A | 0098003 | biological_process | viral tail assembly |
| A | 0098015 | cellular_component | virus tail |
| A | 0098025 | cellular_component | virus tail, baseplate |
| A | 0098932 | biological_process | symbiont entry into host cell via disruption of host cell wall peptidoglycan |
| A | 0098994 | biological_process | symbiont entry into host cell via disruption of host cell envelope |
| D | 0005515 | molecular_function | protein binding |
| D | 0044423 | cellular_component | virion component |
| D | 0098003 | biological_process | viral tail assembly |
| D | 0098015 | cellular_component | virus tail |
| D | 0098025 | cellular_component | virus tail, baseplate |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 A 586 |
| Chain | Residue |
| A | LYS454 |
| A | LYS454 |
| A | LYS454 |
| A | HOH606 |
| A | HOH606 |
| A | HOH606 |
Functional Information from PROSITE/UniProt
| site_id | PS00066 |
| Number of Residues | 15 |
| Details | HMG_COA_REDUCTASE_1 Hydroxymethylglutaryl-coenzyme A reductases signature 1. KfVFvWQDiMGvNmM |
| Chain | Residue | Details |
| D | LYS184-MET198 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_04151","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11823865","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"HAMAP-Rule","id":"MF_04151","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11823865","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Site: {"description":"Cleavage","evidences":[{"source":"HAMAP-Rule","id":"MF_04151","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10217762","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15701513","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 206l |
| Chain | Residue | Details |
| A | ASP193 | |
| A | GLU184 |
