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 |
A | LEU85 | |
B | GLY191 | |
B | ASP222 | |
B | LYS360 | |
A | LYS99 | |
A | GLN162 | |
A | GLY191 | |
A | ASP222 | |
A | LYS360 | |
B | LEU85 | |
B | LYS99 | |
B | GLN162 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q16851 |
Chain | Residue | Details |
A | GLY87 | |
A | HIS192 | |
A | ASN220 | |
B | GLY87 | |
B | HIS192 | |
B | ASN220 |
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 |