5VNR
X-ray structure of perdeuterated T4 lysozyme cysteine-free pseudo-wild type at cryogenic temperature
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003796 | molecular_function | lysozyme activity |
| A | 0003824 | molecular_function | catalytic activity |
| 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 | 0030430 | cellular_component | host cell cytoplasm |
| A | 0031640 | biological_process | killing of cells of another organism |
| A | 0042742 | biological_process | defense response to bacterium |
| A | 0044659 | biological_process | viral release from host cell by cytolysis |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | binding site for residue PO4 A 201 |
| Chain | Residue |
| A | LYS19 |
| A | ARG125 |
| A | TRP126 |
| A | ASP127 |
| A | GLU128 |
| A | HOH304 |
| A | HOH408 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 202 |
| Chain | Residue |
| A | HOH346 |
| A | HOH372 |
| A | HOH407 |
| A | GLU11 |
| A | TYR18 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue HED A 203 |
| Chain | Residue |
| A | PHE4 |
| A | ASP72 |
| A | ALA93 |
| A | ILE100 |
| A | HOH307 |
| A | HOH342 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue CL A 204 |
| Chain | Residue |
| A | LYS124 |
| A | THR142 |
| A | ASN144 |
| A | ARG145 |
| A | HOH582 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 205 |
| Chain | Residue |
| A | HIS31 |
| A | LYS135 |
| A | HOH424 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | binding site for residue GOL A 206 |
| Chain | Residue |
| A | ASP72 |
| A | ARG76 |
| A | LEU79 |
| A | ASP89 |
| A | HOH301 |
| A | HOH302 |
| A | HOH307 |
| A | HOH319 |
| A | HOH355 |
| A | HOH381 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_04110","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"3382407","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_04110","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1892846","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3382407","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 921 |
| Chain | Residue | Details |
| A | GLU11 | proton shuttle (general acid/base) |
| A | ASP20 | covalent catalysis |
