4X6L
Crystal structure of S. aureus TarM in complex with UDP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0019350 | biological_process | teichoic acid biosynthetic process |
| A | 0047269 | molecular_function | poly(ribitol-phosphate) N-acetylglucosaminyltransferase activity |
| A | 0071555 | biological_process | cell wall organization |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0016757 | molecular_function | glycosyltransferase activity |
| B | 0019350 | biological_process | teichoic acid biosynthetic process |
| B | 0047269 | molecular_function | poly(ribitol-phosphate) N-acetylglucosaminyltransferase activity |
| B | 0071555 | biological_process | cell wall organization |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0016757 | molecular_function | glycosyltransferase activity |
| C | 0019350 | biological_process | teichoic acid biosynthetic process |
| C | 0047269 | molecular_function | poly(ribitol-phosphate) N-acetylglucosaminyltransferase activity |
| C | 0071555 | biological_process | cell wall organization |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0016757 | molecular_function | glycosyltransferase activity |
| D | 0019350 | biological_process | teichoic acid biosynthetic process |
| D | 0047269 | molecular_function | poly(ribitol-phosphate) N-acetylglucosaminyltransferase activity |
| D | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | binding site for residue UDP A 500 |
| Chain | Residue |
| A | GLY17 |
| A | LEU407 |
| A | SER408 |
| A | GLU411 |
| A | ILE324 |
| A | ARG326 |
| A | LYS331 |
| A | TYR382 |
| A | THR383 |
| A | PRO386 |
| A | GLU403 |
| A | GLY406 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | binding site for residue UDP B 500 |
| Chain | Residue |
| B | GLY17 |
| B | ILE324 |
| B | ARG326 |
| B | LYS331 |
| B | TYR382 |
| B | THR383 |
| B | PRO386 |
| B | GLY406 |
| B | LEU407 |
| B | SER408 |
| B | GLU411 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | binding site for residue UDP C 500 |
| Chain | Residue |
| C | GLY17 |
| C | ILE324 |
| C | ARG326 |
| C | LYS331 |
| C | TYR382 |
| C | THR383 |
| C | PRO386 |
| C | GLY406 |
| C | LEU407 |
| C | SER408 |
| C | GLU411 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25624472, ECO:0000269|PubMed:25697358 |
| Chain | Residue | Details |
| A | GLY17 | |
| D | GLY17 | |
| D | THR383 | |
| D | GLU403 | |
| A | THR383 | |
| A | GLU403 | |
| B | GLY17 | |
| B | THR383 | |
| B | GLU403 | |
| C | GLY17 | |
| C | THR383 | |
| C | GLU403 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25624472 |
| Chain | Residue | Details |
| A | LYS59 | |
| D | LYS59 | |
| D | ARG326 | |
| D | LYS331 | |
| A | ARG326 | |
| A | LYS331 | |
| B | LYS59 | |
| B | ARG326 | |
| B | LYS331 | |
| C | LYS59 | |
| C | ARG326 | |
| C | LYS331 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25697358 |
| Chain | Residue | Details |
| A | HIS249 | |
| B | HIS249 | |
| C | HIS249 | |
| D | HIS249 |
