1HXQ
THE STRUCTURE OF NUCLEOTIDYLATED GALACTOSE-1-PHOSPHATE URIDYLYLTRANSFERASE FROM ESCHERICHIA COLI AT 1.86 ANGSTROMS RESOLUTION
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004335 | molecular_function | galactokinase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006012 | biological_process | galactose metabolic process |
| A | 0008108 | molecular_function | UDP-glucose:hexose-1-phosphate uridylyltransferase activity |
| A | 0008198 | molecular_function | ferrous iron binding |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0033499 | biological_process | galactose catabolic process via UDP-galactose, Leloir pathway |
| A | 0046835 | biological_process | carbohydrate phosphorylation |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004335 | molecular_function | galactokinase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006012 | biological_process | galactose metabolic process |
| B | 0008108 | molecular_function | UDP-glucose:hexose-1-phosphate uridylyltransferase activity |
| B | 0008198 | molecular_function | ferrous iron binding |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016779 | molecular_function | nucleotidyltransferase activity |
| B | 0033499 | biological_process | galactose catabolic process via UDP-galactose, Leloir pathway |
| B | 0046835 | biological_process | carbohydrate phosphorylation |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 350 |
| Chain | Residue |
| A | CYS52 |
| A | CYS55 |
| A | HIS115 |
| A | HIS164 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE A 351 |
| Chain | Residue |
| A | GLU182 |
| A | HIS281 |
| A | HIS296 |
| A | HIS298 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 350 |
| Chain | Residue |
| B | CYS55 |
| B | HIS115 |
| B | HIS164 |
| B | CYS52 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE B 351 |
| Chain | Residue |
| B | GLU182 |
| B | HIS281 |
| B | HIS296 |
| B | HIS298 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE U5P A 352 |
| Chain | Residue |
| A | ARG60 |
| A | VAL61 |
| A | ASN77 |
| A | ASP78 |
| A | VAL108 |
| A | CYS160 |
| A | HIS166 |
| A | GLN168 |
| A | HOH516 |
| A | HOH518 |
| A | HOH519 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE U5P B 352 |
| Chain | Residue |
| B | PHE53 |
| B | ARG60 |
| B | VAL61 |
| B | ASN77 |
| B | ASP78 |
| B | VAL108 |
| B | CYS160 |
| B | HIS166 |
| B | GLN168 |
| B | HOH359 |
| B | HOH394 |
| B | HOH614 |
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. FENKGaamGcsnpHPHgQ |
| Chain | Residue | Details |
| A | PHE151-GLN168 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Tele-UMP-histidine intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU10033","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"8794735","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9063869","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9063869","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1GUQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8794735","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9063869","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1GUQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1HXQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 14 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"9063869","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1GUQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 8 |
| Details | M-CSA 88 |
| Chain | Residue | Details |
| A | CYS52 | metal ligand |
| A | CYS55 | metal ligand |
| A | HIS115 | metal ligand |
| A | ASN153 | activator, hydrogen bond donor |
| A | SER161 | electrostatic stabiliser, hydrogen bond donor, steric role |
| A | HIS164 | activator |
| A | HIS166 | hydrogen bond donor, nucleofuge, nucleophile |
| A | GLN168 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 8 |
| Details | M-CSA 88 |
| Chain | Residue | Details |
| B | CYS52 | metal ligand |
| B | CYS55 | metal ligand |
| B | HIS115 | metal ligand |
| B | ASN153 | activator, hydrogen bond donor |
| B | SER161 | electrostatic stabiliser, hydrogen bond donor, steric role |
| B | HIS164 | activator |
| B | HIS166 | hydrogen bond donor, nucleofuge, nucleophile |
| B | GLN168 | electrostatic stabiliser, hydrogen bond donor |
