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 | 0009253 | biological_process | peptidoglycan catabolic process |
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 | 0009253 | biological_process | peptidoglycan catabolic process |
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 | 2 |
Details | SITE: Breakpoint for translocation to form ETV6-MDS2 in MDS |
Chain | Residue | Details |
A | LEU22 | |
C | LEU22 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | SITE: Breakpoint for translocation to form PAX5-ETV6 |
Chain | Residue | Details |
A | ARG23 | |
C | ARG23 |
site_id | SWS_FT_FI3 |
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 |
B | GLU104 | |
D | GLU104 |
site_id | SWS_FT_FI4 |
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 |
B | ASP113 | |
D | ASP113 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:8266098 |
Chain | Residue | Details |
B | LEU125 | |
B | PHE197 | |
D | LEU125 | |
D | PHE197 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000303|PubMed:7831309 |
Chain | Residue | Details |
B | SER210 | |
B | ASN225 | |
D | SER210 | |
D | ASN225 |
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 |