6IJ9
Crystal Structure of Arabidopsis thaliana UGT89C1 complexed with UDP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005829 | cellular_component | cytosol |
| A | 0008194 | molecular_function | UDP-glycosyltransferase activity |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0051555 | biological_process | flavonol biosynthetic process |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005829 | cellular_component | cytosol |
| B | 0008194 | molecular_function | UDP-glycosyltransferase activity |
| B | 0016757 | molecular_function | glycosyltransferase activity |
| B | 0051555 | biological_process | flavonol biosynthetic process |
| C | 0005576 | cellular_component | extracellular region |
| C | 0005829 | cellular_component | cytosol |
| C | 0008194 | molecular_function | UDP-glycosyltransferase activity |
| C | 0016757 | molecular_function | glycosyltransferase activity |
| C | 0051555 | biological_process | flavonol biosynthetic process |
| D | 0005576 | cellular_component | extracellular region |
| D | 0005829 | cellular_component | cytosol |
| D | 0008194 | molecular_function | UDP-glycosyltransferase activity |
| D | 0016757 | molecular_function | glycosyltransferase activity |
| D | 0051555 | biological_process | flavonol biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | binding site for residue UDP A 900 |
| Chain | Residue |
| A | GLN18 |
| A | SER337 |
| A | GLU340 |
| A | GLY20 |
| A | ARG219 |
| A | SER250 |
| A | TRP314 |
| A | ALA315 |
| A | GLN317 |
| A | HIS332 |
| A | GLY336 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | binding site for residue UDP B 900 |
| Chain | Residue |
| B | GLY20 |
| B | ARG219 |
| B | SER250 |
| B | GLN251 |
| B | TRP314 |
| B | ALA315 |
| B | GLN317 |
| B | HIS332 |
| B | GLY336 |
| B | SER337 |
| B | GLU340 |
| B | HOH1005 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | binding site for residue UDP C 900 |
| Chain | Residue |
| C | GLN18 |
| C | GLY20 |
| C | ARG219 |
| C | GLY249 |
| C | SER250 |
| C | TRP314 |
| C | ALA315 |
| C | GLN317 |
| C | THR318 |
| C | HIS332 |
| C | GLY336 |
| C | SER337 |
| C | GLU340 |
| C | HOH1004 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | binding site for residue UDP D 900 |
| Chain | Residue |
| D | GLN18 |
| D | GLY20 |
| D | GLY249 |
| D | SER250 |
| D | TRP314 |
| D | ALA315 |
| D | GLN317 |
| D | HIS332 |
| D | GLY336 |
| D | SER337 |
| D | GLU340 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:A0A0A1HA03 |
| Chain | Residue | Details |
| A | HIS21 | |
| B | HIS21 | |
| C | HIS21 | |
| D | HIS21 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Charge relay => ECO:0000250|UniProtKB:A0A0A1HA03 |
| Chain | Residue | Details |
| A | ASP119 | |
| B | ASP119 | |
| C | ASP119 | |
| D | ASP119 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 28 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:30893500, ECO:0007744|PDB:6IJA |
| Chain | Residue | Details |
| A | GLN18 | |
| B | ALA315 | |
| B | HIS332 | |
| B | GLY336 | |
| B | SER337 | |
| B | GLU340 | |
| C | GLN18 | |
| C | SER250 | |
| C | ALA315 | |
| C | HIS332 | |
| C | GLY336 | |
| A | SER250 | |
| C | SER337 | |
| C | GLU340 | |
| D | GLN18 | |
| D | SER250 | |
| D | ALA315 | |
| D | HIS332 | |
| D | GLY336 | |
| D | SER337 | |
| D | GLU340 | |
| A | ALA315 | |
| A | HIS332 | |
| A | GLY336 | |
| A | SER337 | |
| A | GLU340 | |
| B | GLN18 | |
| B | SER250 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:30893500, ECO:0007744|PDB:6IJD |
| Chain | Residue | Details |
| A | HIS21 | |
| B | HIS21 | |
| C | HIS21 | |
| D | HIS21 |
