3M2P
The crystal structure of UDP-N-acetylglucosamine 4-epimerase from Bacillus cereus
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0003974 | molecular_function | UDP-N-acetylglucosamine 4-epimerase activity |
A | 0016853 | molecular_function | isomerase activity |
B | 0000166 | molecular_function | nucleotide binding |
B | 0003974 | molecular_function | UDP-N-acetylglucosamine 4-epimerase activity |
B | 0016853 | molecular_function | isomerase activity |
C | 0000166 | molecular_function | nucleotide binding |
C | 0003974 | molecular_function | UDP-N-acetylglucosamine 4-epimerase activity |
C | 0016853 | molecular_function | isomerase activity |
D | 0000166 | molecular_function | nucleotide binding |
D | 0003974 | molecular_function | UDP-N-acetylglucosamine 4-epimerase activity |
D | 0016853 | molecular_function | isomerase activity |
E | 0000166 | molecular_function | nucleotide binding |
E | 0003974 | molecular_function | UDP-N-acetylglucosamine 4-epimerase activity |
E | 0016853 | molecular_function | isomerase activity |
F | 0000166 | molecular_function | nucleotide binding |
F | 0003974 | molecular_function | UDP-N-acetylglucosamine 4-epimerase activity |
F | 0016853 | molecular_function | isomerase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE UDP B 7517 |
Chain | Residue |
B | GLY7 |
B | THR9 |
B | GLY10 |
B | PHE11 |
B | LEU12 |
B | ARG32 |
B | ALA69 |
B | THR70 |
B | HOH321 |