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 |