4TN3
Structure of the BBox-Coiled-coil region of Rhesus Trim5alpha
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003796 | molecular_function | lysozyme activity |
A | 0008270 | molecular_function | zinc ion binding |
A | 0009253 | biological_process | peptidoglycan catabolic process |
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 |
B | 0003796 | molecular_function | lysozyme activity |
B | 0008270 | molecular_function | zinc ion binding |
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 | 0044659 | biological_process | viral release from host cell by cytolysis |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue ZN A 701 |
Chain | Residue |
A | CYS108 |
A | ASP111 |
A | GLU124 |
A | HIS125 |
A | HIS128 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue ZN A 702 |
Chain | Residue |
A | CYS97 |
A | HIS100 |
A | CYS116 |
A | CYS119 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue ZN B 700 |
Chain | Residue |
B | CYS108 |
B | ASP111 |
B | HIS125 |
B | HIS128 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue ZN B 701 |
Chain | Residue |
B | CYS97 |
B | HIS100 |
B | CYS116 |
B | CYS119 |
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 |
A | GLU314 | |
B | GLU314 |
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 |
A | ASN323 | |
B | ASN323 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:8266098 |
Chain | Residue | Details |
A | LEU335 | |
A | PHE407 | |
B | LEU335 | |
B | PHE407 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000303|PubMed:7831309 |
Chain | Residue | Details |
A | SER420 | |
A | ASN435 | |
B | SER420 | |
B | ASN435 |