6K8D
UDP-glucose pyrophosphorylase with UPG from Acinetobacter Baumanii
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003983 | molecular_function | UTP:glucose-1-phosphate uridylyltransferase activity |
A | 0006011 | biological_process | UDP-glucose metabolic process |
A | 0009058 | biological_process | biosynthetic process |
A | 0016779 | molecular_function | nucleotidyltransferase activity |
B | 0003983 | molecular_function | UTP:glucose-1-phosphate uridylyltransferase activity |
B | 0006011 | biological_process | UDP-glucose metabolic process |
B | 0009058 | biological_process | biosynthetic process |
B | 0016779 | molecular_function | nucleotidyltransferase activity |
C | 0003983 | molecular_function | UTP:glucose-1-phosphate uridylyltransferase activity |
C | 0006011 | biological_process | UDP-glucose metabolic process |
C | 0009058 | biological_process | biosynthetic process |
C | 0016779 | molecular_function | nucleotidyltransferase activity |
D | 0003983 | molecular_function | UTP:glucose-1-phosphate uridylyltransferase activity |
D | 0006011 | biological_process | UDP-glucose metabolic process |
D | 0009058 | biological_process | biosynthetic process |
D | 0016779 | molecular_function | nucleotidyltransferase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 17 |
Details | binding site for residue UPG A 301 |
Chain | Residue |
A | PRO7 |
A | ALA111 |
A | LEU128 |
A | PRO129 |
A | ASP130 |
A | GLY171 |
A | GLU192 |
A | VAL205 |
A | THR233 |
A | VAL8 |
A | ALA9 |
A | GLY10 |
A | GLN102 |
A | PRO105 |
A | LEU106 |
A | GLY107 |
A | LEU108 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue SO4 A 302 |
Chain | Residue |
A | GLY10 |
A | LEU11 |
A | THR13 |
site_id | AC3 |
Number of Residues | 2 |
Details | binding site for residue SO4 A 303 |
Chain | Residue |
A | GLN139 |
A | ARG144 |
site_id | AC4 |
Number of Residues | 1 |
Details | binding site for residue EDO A 304 |
Chain | Residue |
A | HIS110 |
site_id | AC5 |
Number of Residues | 17 |
Details | binding site for residue UPG B 301 |
Chain | Residue |
B | PRO7 |
B | VAL8 |
B | ALA9 |
B | GLY10 |
B | GLN102 |
B | PRO105 |
B | LEU106 |
B | GLY107 |
B | LEU108 |
B | LEU128 |
B | PRO129 |
B | ASP130 |
B | GLY171 |
B | GLU192 |
B | VAL205 |
B | THR233 |
B | SO4303 |
site_id | AC6 |
Number of Residues | 2 |
Details | binding site for residue SO4 B 302 |
Chain | Residue |
A | GLN104 |
B | ARG67 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue SO4 B 303 |
Chain | Residue |
B | LEU11 |
B | GLY12 |
B | THR13 |
B | UPG301 |
site_id | AC8 |
Number of Residues | 2 |
Details | binding site for residue GOL B 304 |
Chain | Residue |
B | GLN139 |
B | ARG144 |
site_id | AC9 |
Number of Residues | 17 |
Details | binding site for residue UPG C 301 |
Chain | Residue |
C | PRO7 |
C | VAL8 |
C | ALA9 |
C | GLY10 |
C | LYS24 |
C | GLN102 |
C | PRO105 |
C | LEU106 |
C | GLY107 |
C | LEU108 |
C | LEU128 |
C | ASP130 |
C | TYR170 |
C | GLY171 |
C | GLU192 |
C | VAL205 |
C | VAL206 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue SO4 C 302 |
Chain | Residue |
A | LYS78 |
C | LEU11 |
C | GLY12 |
C | THR13 |
site_id | AD2 |
Number of Residues | 17 |
Details | binding site for residue UPG D 301 |
Chain | Residue |
D | PRO7 |
D | VAL8 |
D | ALA9 |
D | GLY10 |
D | LYS24 |
D | GLN102 |
D | PRO105 |
D | LEU106 |
D | GLY107 |
D | LEU108 |
D | LEU128 |
D | ASP130 |
D | TYR170 |
D | GLY171 |
D | GLU192 |
D | VAL205 |
D | VAL206 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue SO4 D 302 |
Chain | Residue |
D | LEU11 |
D | GLY12 |
D | THR13 |
D | ARG14 |
site_id | AD4 |
Number of Residues | 1 |
Details | binding site for residue SO4 D 303 |
Chain | Residue |
D | LYS116 |
Functional Information from PROSITE/UniProt
site_id | PS00783 |
Number of Residues | 23 |
Details | RIBOSOMAL_L13 Ribosomal protein L13 signature. LSRMISryns.SQaaqimVeAVpD |
Chain | Residue | Details |
A | LEU142-ASP164 |