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 | 0003824 | molecular_function | catalytic activity |
| A | 0008152 | biological_process | metabolic process |
| A | 0008270 | molecular_function | zinc ion binding |
| 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 |
| B | 0003796 | molecular_function | lysozyme activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0008152 | biological_process | metabolic process |
| B | 0008270 | molecular_function | zinc ion binding |
| 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 | 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 |
