5IN3
Crystal structure of glucose-1-phosphate bound nucleotidylated human galactose-1-phosphate uridylyltransferase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005515 | molecular_function | protein binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005794 | cellular_component | Golgi apparatus |
A | 0005829 | cellular_component | cytosol |
A | 0006011 | biological_process | UDP-glucose metabolic process |
A | 0006012 | biological_process | galactose metabolic process |
A | 0008108 | molecular_function | UDP-glucose:hexose-1-phosphate uridylyltransferase activity |
A | 0008270 | molecular_function | zinc ion binding |
A | 0016779 | molecular_function | nucleotidyltransferase activity |
A | 0033499 | biological_process | galactose catabolic process via UDP-galactose |
A | 0046872 | molecular_function | metal ion binding |
B | 0005515 | molecular_function | protein binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005794 | cellular_component | Golgi apparatus |
B | 0005829 | cellular_component | cytosol |
B | 0006011 | biological_process | UDP-glucose metabolic process |
B | 0006012 | biological_process | galactose metabolic process |
B | 0008108 | molecular_function | UDP-glucose:hexose-1-phosphate uridylyltransferase activity |
B | 0008270 | molecular_function | zinc ion binding |
B | 0016779 | molecular_function | nucleotidyltransferase activity |
B | 0033499 | biological_process | galactose catabolic process via UDP-galactose |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PROSITE/UniProt
site_id | PS00117 |
Number of Residues | 18 |
Details | GAL_P_UDP_TRANSF_I Galactose-1-phosphate uridyl transferase family 1 active site signature. FENKGammGcsnpHPHcQ |
Chain | Residue | Details |
B | PHE171-GLN188 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Tele-UMP-histidine intermediate => ECO:0000255|PROSITE-ProRule:PRU10033, ECO:0000269|PubMed:27005423 |
Chain | Residue | Details |
B | HIS186 | |
A | HIS186 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU10033 |
Chain | Residue | Details |
B | CYS75 | |
B | HIS184 | |
A | CYS75 | |
A | HIS184 |
site_id | SWS_FT_FI3 |
Number of Residues | 10 |
Details | BINDING: in other chain => ECO:0000305|PubMed:27005423 |
Chain | Residue | Details |
B | ALA81 | |
A | TYR339 | |
B | ASN97 | |
B | GLN188 | |
B | LYS334 | |
B | TYR339 | |
A | ALA81 | |
A | ASN97 | |
A | GLN188 | |
A | LYS334 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000305|PubMed:27005423 |
Chain | Residue | Details |
B | ASN173 | |
A | ASN173 |
site_id | SWS_FT_FI5 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:27005423 |
Chain | Residue | Details |
B | GLU202 | |
B | HIS301 | |
B | HIS319 | |
B | HIS321 | |
A | GLU202 | |
A | HIS301 | |
A | HIS319 | |
A | HIS321 |