2PA4
Crystal structure of UDP-glucose pyrophosphorylase from Corynebacteria glutamicum in complex with magnesium and UDP-glucose
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003983 | molecular_function | UTP:glucose-1-phosphate uridylyltransferase activity |
| A | 0006011 | biological_process | UDP-alpha-D-glucose metabolic process |
| A | 0009058 | biological_process | biosynthetic process |
| B | 0003983 | molecular_function | UTP:glucose-1-phosphate uridylyltransferase activity |
| B | 0006011 | biological_process | UDP-alpha-D-glucose metabolic process |
| B | 0009058 | biological_process | biosynthetic process |
| C | 0003983 | molecular_function | UTP:glucose-1-phosphate uridylyltransferase activity |
| C | 0006011 | biological_process | UDP-alpha-D-glucose metabolic process |
| C | 0009058 | biological_process | biosynthetic process |
| D | 0003983 | molecular_function | UTP:glucose-1-phosphate uridylyltransferase activity |
| D | 0006011 | biological_process | UDP-alpha-D-glucose metabolic process |
| D | 0009058 | biological_process | biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 324 |
| Chain | Residue |
| A | UPG326 |
| A | HOH332 |
| A | HOH333 |
| A | HOH334 |
| A | HOH335 |
| A | HOH405 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 325 |
| Chain | Residue |
| A | HOH337 |
| A | HOH363 |
| A | ASP142 |
| A | UPG326 |
| A | HOH336 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 324 |
| Chain | Residue |
| B | UPG326 |
| B | HOH331 |
| B | HOH332 |
| B | HOH333 |
| B | HOH379 |
| B | HOH380 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 325 |
| Chain | Residue |
| B | ASP142 |
| B | UPG326 |
| B | HOH335 |
| B | HOH336 |
| B | HOH382 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG C 324 |
| Chain | Residue |
| C | UPG326 |
| C | HOH332 |
| C | HOH333 |
| C | HOH404 |
| C | HOH405 |
| C | HOH407 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 325 |
| Chain | Residue |
| C | ASP142 |
| C | UPG326 |
| C | HOH336 |
| C | HOH408 |
| C | HOH409 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG D 324 |
| Chain | Residue |
| D | UPG326 |
| D | HOH332 |
| D | HOH333 |
| D | HOH339 |
| D | HOH350 |
| D | HOH351 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG D 325 |
| Chain | Residue |
| D | LYS35 |
| D | ASP142 |
| D | UPG326 |
| D | HOH335 |
| D | HOH336 |
| D | HOH349 |
| site_id | AC9 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE UPG A 326 |
| Chain | Residue |
| A | PRO18 |
| A | ALA19 |
| A | ALA20 |
| A | GLY21 |
| A | LYS35 |
| A | GLU36 |
| A | GLN112 |
| A | PRO115 |
| A | LEU116 |
| A | GLY117 |
| A | LEU118 |
| A | ALA121 |
| A | LEU140 |
| A | PRO141 |
| A | ASP142 |
| A | ASP143 |
| A | TYR179 |
| A | GLY180 |
| A | GLU201 |
| A | LYS202 |
| A | ALA214 |
| A | THR242 |
| A | ARG264 |
| A | MG324 |
| A | MG325 |
| A | HOH330 |
| A | HOH332 |
| A | HOH334 |
| A | HOH335 |
| A | HOH336 |
| A | HOH337 |
| A | HOH363 |
| A | HOH366 |
| A | HOH475 |
| site_id | BC1 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE UPG B 326 |
| Chain | Residue |
| B | ALA214 |
| B | GLY216 |
| B | THR242 |
| B | MG324 |
| B | MG325 |
| B | HOH329 |
| B | HOH331 |
| B | HOH335 |
| B | HOH336 |
| B | HOH352 |
| B | HOH379 |
| B | HOH380 |
| B | HOH382 |
| B | HOH399 |
| B | HOH402 |
| B | PRO18 |
| B | ALA19 |
| B | ALA20 |
| B | GLY21 |
| B | LYS35 |
| B | GLU36 |
| B | GLN112 |
| B | PRO115 |
| B | LEU116 |
| B | GLY117 |
| B | LEU118 |
| B | ALA121 |
| B | LEU140 |
| B | PRO141 |
| B | ASP142 |
| B | ASP143 |
| B | TYR179 |
| B | GLY180 |
| B | GLU201 |
| B | LYS202 |
| site_id | BC2 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE UPG C 326 |
| Chain | Residue |
| C | PRO18 |
| C | ALA19 |
| C | ALA20 |
| C | GLY21 |
| C | LYS35 |
| C | GLU36 |
| C | GLN112 |
| C | PRO115 |
| C | LEU116 |
| C | GLY117 |
| C | LEU118 |
| C | ALA121 |
| C | LEU140 |
| C | PRO141 |
| C | ASP142 |
| C | ASP143 |
| C | TYR179 |
| C | GLY180 |
| C | GLU201 |
| C | LYS202 |
| C | ALA214 |
| C | THR242 |
| C | MG324 |
| C | MG325 |
| C | HOH332 |
| C | HOH333 |
| C | HOH336 |
| C | HOH402 |
| C | HOH404 |
| C | HOH406 |
| C | HOH407 |
| C | HOH408 |
| C | HOH409 |
| C | HOH412 |
| site_id | BC3 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE UPG D 326 |
| Chain | Residue |
| D | PRO18 |
| D | ALA19 |
| D | ALA20 |
| D | GLY21 |
| D | LYS35 |
| D | GLU36 |
| D | GLN112 |
| D | PRO115 |
| D | LEU116 |
| D | GLY117 |
| D | LEU118 |
| D | ALA121 |
| D | LEU140 |
| D | PRO141 |
| D | ASP142 |
| D | ASP143 |
| D | TYR179 |
| D | GLY180 |
| D | GLU201 |
| D | LYS202 |
| D | ALA214 |
| D | THR215 |
| D | GLY216 |
| D | THR242 |
| D | MG324 |
| D | MG325 |
| D | HOH330 |
| D | HOH333 |
| D | HOH335 |
| D | HOH336 |
| D | HOH339 |
| D | HOH349 |
| D | HOH350 |
| D | HOH351 |
| D | HOH392 |
| D | HOH412 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1hv9 |
| Chain | Residue | Details |
| A | ARG25 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1hv9 |
| Chain | Residue | Details |
| B | ARG25 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1hv9 |
| Chain | Residue | Details |
| C | ARG25 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1hv9 |
| Chain | Residue | Details |
| D | ARG25 |
