2QB0
Structure of the 2TEL crystallization module fused to T4 lysozyme with an Ala-Gly-Pro linker.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0043565 | molecular_function | sequence-specific DNA binding |
| B | 0003796 | molecular_function | lysozyme activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0009253 | biological_process | peptidoglycan catabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0016998 | biological_process | cell wall macromolecule catabolic process |
| B | 0030430 | cellular_component | host cell cytoplasm |
| B | 0031640 | biological_process | killing of cells of another organism |
| B | 0042742 | biological_process | defense response to bacterium |
| B | 0043565 | molecular_function | sequence-specific DNA binding |
| B | 0044659 | biological_process | viral release from host cell by cytolysis |
| C | 0043565 | molecular_function | sequence-specific DNA binding |
| D | 0003796 | molecular_function | lysozyme activity |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0009253 | biological_process | peptidoglycan catabolic process |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| D | 0016998 | biological_process | cell wall macromolecule catabolic process |
| D | 0030430 | cellular_component | host cell cytoplasm |
| D | 0031640 | biological_process | killing of cells of another organism |
| D | 0042742 | biological_process | defense response to bacterium |
| D | 0043565 | molecular_function | sequence-specific DNA binding |
| D | 0044659 | biological_process | viral release from host cell by cytolysis |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MN D 256 |
| Chain | Residue |
| D | GLU104 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MN B 256 |
| Chain | Residue |
| B | GLU104 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN B 257 |
| Chain | Residue |
| B | HIS21 |
| B | ASP33 |
| B | ASP154 |
| B | GLU157 |
| B | HOH277 |
| B | HOH286 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MN C 207 |
| Chain | Residue |
| C | HIS76 |
| C | SER74 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN D 257 |
| Chain | Residue |
| D | ASP33 |
| D | ASP154 |
| D | GLU157 |
| D | HOH276 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Site: {"description":"Breakpoint for translocation to form ETV6-MDS2 in MDS"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Site: {"description":"Breakpoint for translocation to form PAX5-ETV6"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| 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_FI4 |
| Number of Residues | 2 |
| 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_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000303"}]} |
| 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 |
| B | GLU104 | |
| B | ASP113 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 206l |
| Chain | Residue | Details |
| D | GLU104 | |
| D | ASP113 |
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 921 |
| Chain | Residue | Details |
| B | GLU104 | proton shuttle (general acid/base) |
| B | ASP113 | covalent catalysis |
| site_id | MCSA2 |
| Number of Residues | 2 |
| Details | M-CSA 921 |
| Chain | Residue | Details |
| D | GLU104 | proton shuttle (general acid/base) |
| D | ASP113 | covalent catalysis |
