2QAR
Structure of the 2TEL crystallization module fused to T4 lysozyme with a helical linker.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0043565 | molecular_function | sequence-specific DNA binding |
| B | 0043565 | molecular_function | sequence-specific DNA binding |
| C | 0003796 | molecular_function | lysozyme activity |
| C | 0009253 | biological_process | peptidoglycan catabolic process |
| C | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| C | 0016998 | biological_process | cell wall macromolecule catabolic process |
| C | 0030430 | cellular_component | host cell cytoplasm |
| C | 0031640 | biological_process | killing of cells of another organism |
| C | 0042742 | biological_process | defense response to bacterium |
| C | 0044659 | biological_process | viral release from host cell by cytolysis |
| D | 0043565 | molecular_function | sequence-specific DNA binding |
| E | 0043565 | molecular_function | sequence-specific DNA binding |
| F | 0003796 | molecular_function | lysozyme activity |
| F | 0009253 | biological_process | peptidoglycan catabolic process |
| F | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| F | 0016998 | biological_process | cell wall macromolecule catabolic process |
| F | 0030430 | cellular_component | host cell cytoplasm |
| F | 0031640 | biological_process | killing of cells of another organism |
| F | 0042742 | biological_process | defense response to bacterium |
| F | 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 NO3 A 102 |
| Chain | Residue |
| A | GLN25 |
| A | PRO26 |
| A | ILE27 |
| A | LEU63 |
| A | LEU89 |
| A | GLY95 |
| A | GLY96 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NH4 A 201 |
| Chain | Residue |
| A | LEU65 |
| A | PHE70 |
| A | LEU85 |
| A | LEU62 |
| A | LEU63 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NO3 B 109 |
| Chain | Residue |
| B | ARG23 |
| E | LEU24 |
| E | HOH116 |
| E | HOH127 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NO3 D 101 |
| Chain | Residue |
| D | GLN25 |
| D | PRO26 |
| D | ILE27 |
| D | LEU89 |
| D | GLY95 |
| D | GLY96 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NO3 D 104 |
| Chain | Residue |
| C | ASP62 |
| C | LYS66 |
| D | ARG23 |
| D | TYR28 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NO3 D 106 |
| Chain | Residue |
| D | PRO19 |
| D | ALA20 |
| D | HIS21 |
| D | LEU22 |
| D | TRP40 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NO3 D 108 |
| Chain | Residue |
| D | GLU68 |
| E | LYS67 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NH4 D 202 |
| Chain | Residue |
| D | LEU62 |
| D | LEU63 |
| D | LEU65 |
| D | PHE70 |
| D | LEU85 |
| D | HOH210 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NO3 E 108 |
| Chain | Residue |
| E | GLN25 |
| E | PRO26 |
| E | ILE27 |
| E | LEU89 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NO3 E 109 |
| Chain | Residue |
| D | ALA14 |
| D | HIS87 |
| D | HOH214 |
| E | LYS60 |
| E | LEU64 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098 |
| Chain | Residue | Details |
| C | GLU12 | |
| F | GLU12 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:1892846, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098 |
| Chain | Residue | Details |
| C | ASP21 | |
| F | ASP21 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:8266098 |
| Chain | Residue | Details |
| C | LEU33 | |
| C | PHE105 | |
| F | LEU33 | |
| F | PHE105 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000303|PubMed:7831309 |
| Chain | Residue | Details |
| C | SER118 | |
| C | ASN133 | |
| F | SER118 | |
| F | ASN133 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 206l |
| Chain | Residue | Details |
| C | ASP21 | |
| C | GLU12 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 206l |
| Chain | Residue | Details |
| F | ASP21 | |
| F | GLU12 |
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 921 |
| Chain | Residue | Details |
| C | GLU12 | proton shuttle (general acid/base) |
| C | ASP21 | covalent catalysis |
| site_id | MCSA2 |
| Number of Residues | 2 |
| Details | M-CSA 921 |
| Chain | Residue | Details |
| F | GLU12 | proton shuttle (general acid/base) |
| F | ASP21 | covalent catalysis |
