3JUK
The Crystal Structure of UDP-glucose pyrophosphorylase complexed with 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-glucose metabolic process |
A | 0009058 | biological_process | biosynthetic process |
A | 0016779 | molecular_function | nucleotidyltransferase activity |
A | 0046872 | molecular_function | metal ion binding |
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 |
B | 0046872 | molecular_function | metal ion binding |
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 |
C | 0046872 | molecular_function | metal ion binding |
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 |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 30 |
Details | BINDING SITE FOR RESIDUE UPG A 282 |
Chain | Residue |
A | PRO8 |
A | LEU108 |
A | ALA111 |
A | LEU128 |
A | ASP130 |
A | ASP131 |
A | TYR170 |
A | GLY171 |
A | GLU190 |
A | LYS191 |
A | VAL203 |
A | ALA10 |
A | THR231 |
A | ARG252 |
A | HOH291 |
A | HOH292 |
A | MG301 |
A | HOH326 |
A | HOH338 |
A | HOH340 |
A | HOH348 |
A | HOH359 |
A | GLY11 |
A | HOH369 |
A | LYS25 |
A | GLU26 |
A | GLN102 |
A | MET105 |
A | LYS106 |
A | GLY107 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 301 |
Chain | Residue |
A | LYS25 |
A | ASP130 |
A | UPG282 |
A | HOH338 |
A | HOH346 |
A | HOH359 |
site_id | AC3 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE MG A 302 |
Chain | Residue |
A | VAL258 |
site_id | AC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE MG A 303 |
Chain | Residue |
A | THR14 |
site_id | AC5 |
Number of Residues | 30 |
Details | BINDING SITE FOR RESIDUE UPG B 282 |
Chain | Residue |
B | PRO8 |
B | ALA9 |
B | ALA10 |
B | GLY11 |
B | LYS25 |
B | GLU26 |
B | GLN102 |
B | MET105 |
B | LYS106 |
B | GLY107 |
B | LEU108 |
B | ALA111 |
B | LEU128 |
B | ASP130 |
B | ASP131 |
B | TYR170 |
B | GLY171 |
B | GLU190 |
B | LYS191 |
B | VAL203 |
B | THR231 |
B | MG304 |
B | HOH311 |
B | HOH314 |
B | HOH320 |
B | HOH333 |
B | HOH360 |
B | HOH407 |
B | HOH531 |
B | HOH558 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 304 |
Chain | Residue |
B | ASP130 |
B | UPG282 |
B | HOH354 |
B | HOH360 |
B | HOH558 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG B 305 |
Chain | Residue |
A | ARG272 |
A | HOH648 |
B | VAL258 |
site_id | AC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE MG B 306 |
Chain | Residue |
B | THR14 |
B | ARG15 |
site_id | AC9 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE UPG C 283 |
Chain | Residue |
C | MG307 |
C | HOH325 |
C | HOH331 |
C | HOH352 |
C | HOH356 |
C | HOH385 |
C | HOH430 |
C | HOH483 |
C | PRO8 |
C | ALA9 |
C | ALA10 |
C | GLY11 |
C | LYS25 |
C | GLU26 |
C | GLN102 |
C | MET105 |
C | LYS106 |
C | GLY107 |
C | LEU108 |
C | ALA111 |
C | LEU128 |
C | ASP130 |
C | ASP131 |
C | TYR170 |
C | GLY171 |
C | GLU190 |
C | LYS191 |
C | VAL203 |
C | THR231 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG C 307 |
Chain | Residue |
C | LYS25 |
C | ASP130 |
C | UPG283 |
C | HOH326 |
C | HOH356 |
C | HOH430 |
site_id | BC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE MG C 309 |
Chain | Residue |
C | SER257 |
C | VAL258 |
site_id | BC3 |
Number of Residues | 31 |
Details | BINDING SITE FOR RESIDUE UPG D 284 |
Chain | Residue |
D | PRO8 |
D | ALA9 |
D | ALA10 |
D | GLY11 |
D | LYS25 |
D | GLU26 |
D | GLN102 |
D | MET105 |
D | LYS106 |
D | GLY107 |
D | LEU108 |
D | ALA111 |
D | LEU128 |
D | ASP130 |
D | ASP131 |
D | TYR170 |
D | GLY171 |
D | GLU190 |
D | LYS191 |
D | VAL203 |
D | THR231 |
D | HOH300 |
D | MG310 |
D | HOH316 |
D | HOH337 |
D | HOH362 |
D | HOH367 |
D | HOH387 |
D | HOH443 |
D | HOH559 |
D | HOH595 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG D 310 |
Chain | Residue |
D | ASP130 |
D | UPG284 |
D | HOH367 |
D | HOH387 |
D | HOH559 |
site_id | BC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE MG D 311 |
Chain | Residue |
D | THR14 |
D | ARG15 |
site_id | BC6 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE MG D 312 |
Chain | Residue |
D | VAL258 |