2ICX
Crystal Structure of a Putative UDP-glucose Pyrophosphorylase from Arabidopsis Thaliana with Bound UTP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003983 | molecular_function | UTP:glucose-1-phosphate uridylyltransferase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0005985 | biological_process | sucrose metabolic process |
| A | 0006011 | biological_process | UDP-glucose metabolic process |
| A | 0009555 | biological_process | pollen development |
| A | 0016036 | biological_process | cellular response to phosphate starvation |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0052543 | biological_process | callose deposition in cell wall |
| A | 0070569 | molecular_function | uridylyltransferase activity |
| A | 0090406 | cellular_component | pollen tube |
| B | 0003983 | molecular_function | UTP:glucose-1-phosphate uridylyltransferase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0005985 | biological_process | sucrose metabolic process |
| B | 0006011 | biological_process | UDP-glucose metabolic process |
| B | 0009555 | biological_process | pollen development |
| B | 0016036 | biological_process | cellular response to phosphate starvation |
| B | 0016779 | molecular_function | nucleotidyltransferase activity |
| B | 0052543 | biological_process | callose deposition in cell wall |
| B | 0070569 | molecular_function | uridylyltransferase activity |
| B | 0090406 | cellular_component | pollen tube |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE DMS A 900 |
| Chain | Residue |
| A | ARG353 |
| A | SER354 |
| A | PHE356 |
| A | ARG382 |
| A | PRO389 |
| A | ASN391 |
| A | HOH962 |
| A | HOH1111 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE UTP A 901 |
| Chain | Residue |
| A | ASN86 |
| A | GLY87 |
| A | GLY88 |
| A | THR92 |
| A | LYS99 |
| A | GLN162 |
| A | PRO189 |
| A | GLY191 |
| A | HIS192 |
| A | ASN220 |
| A | SER221 |
| A | ASP222 |
| A | LYS360 |
| A | HOH1015 |
| A | HOH1030 |
| A | HOH1323 |
| A | HOH1325 |
| A | LEU85 |
| site_id | AC3 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE UTP B 902 |
| Chain | Residue |
| B | LEU85 |
| B | ASN86 |
| B | GLY87 |
| B | GLY88 |
| B | THR92 |
| B | LYS99 |
| B | MET134 |
| B | GLN162 |
| B | PRO189 |
| B | GLY191 |
| B | HIS192 |
| B | ASN220 |
| B | SER221 |
| B | ASP222 |
| B | LYS360 |
| B | HOH1024 |
| B | HOH1111 |
| B | HOH1135 |
| B | HOH1220 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17178129, ECO:0007744|PDB:2ICX |
| Chain | Residue | Details |
| B | GLN162 | |
| B | GLY191 | |
| B | ASP222 | |
| B | LYS360 | |
| A | LEU85 | |
| A | LYS99 | |
| A | GLN162 | |
| A | GLY191 | |
| A | ASP222 | |
| A | LYS360 | |
| B | LEU85 | |
| B | LYS99 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q16851 |
| Chain | Residue | Details |
| A | ASN220 | |
| B | GLY87 | |
| B | HIS192 | |
| B | ASN220 | |
| A | GLY87 | |
| A | HIS192 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylalanine => ECO:0007744|PubMed:22223895 |
| Chain | Residue | Details |
| A | ALA2 | |
| B | ALA2 |
