6IJ7
Crystal Structure of Arabidopsis thaliana UGT89C1
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 |
| A | 0103077 | molecular_function | quercetin 3-glucoside 7-O-rhamnosyltransferase activity |
| A | 0103078 | molecular_function | quercetin 3-rhamnoside 7-O-rhamnosyltransferase activity |
| 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 |
| B | 0103077 | molecular_function | quercetin 3-glucoside 7-O-rhamnosyltransferase activity |
| B | 0103078 | molecular_function | quercetin 3-rhamnoside 7-O-rhamnosyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 501 |
| Chain | Residue |
| A | GLY247 |
| A | GLY249 |
| A | TYR329 |
| A | THR331 |
| A | HIS332 |
| A | GLY334 |
| A | SER337 |
| A | HIS357 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue GOL A 502 |
| Chain | Residue |
| B | LYS411 |
| A | HIS202 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue GOL A 503 |
| Chain | Residue |
| A | LYS411 |
| A | HOH603 |
| B | HIS202 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 504 |
| Chain | Residue |
| A | THR193 |
| A | ARG197 |
| A | EDO505 |
| B | THR193 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 505 |
| Chain | Residue |
| A | LYS367 |
| A | EDO504 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 506 |
| Chain | Residue |
| A | LEU186 |
| A | GLU187 |
| A | PRO188 |
| A | GLU189 |
| A | LEU368 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 507 |
| Chain | Residue |
| A | GLU192 |
| A | LYS195 |
| B | ASP185 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | binding site for residue GOL B 501 |
| Chain | Residue |
| B | GLY247 |
| B | GLY249 |
| B | SER250 |
| B | THR331 |
| B | HIS332 |
| B | GLY334 |
| B | SER337 |
| B | HIS357 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | binding site for residue EDO B 502 |
| Chain | Residue |
| A | ARG197 |
| B | LYS367 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 503 |
| Chain | Residue |
| A | TYR184 |
| A | ASP185 |
| B | GLU192 |
| B | LYS195 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 504 |
| Chain | Residue |
| B | LEU186 |
| B | GLU187 |
| B | PRO188 |
| B | GLU189 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:A0A0A1HA03 |
| Chain | Residue | Details |
| A | HIS21 | |
| B | HIS21 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Charge relay => ECO:0000250|UniProtKB:A0A0A1HA03 |
| Chain | Residue | Details |
| A | ASP119 | |
| B | ASP119 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 14 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:30893500, ECO:0007744|PDB:6IJA |
| Chain | Residue | Details |
| A | GLN18 | |
| A | SER250 | |
| A | ALA315 | |
| A | HIS332 | |
| A | GLY336 | |
| A | SER337 | |
| A | GLU340 | |
| B | GLN18 | |
| B | SER250 | |
| B | ALA315 | |
| B | HIS332 | |
| B | GLY336 | |
| B | SER337 | |
| B | GLU340 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:30893500, ECO:0007744|PDB:6IJD |
| Chain | Residue | Details |
| A | HIS21 | |
| B | HIS21 |
