4LIS
Crystal Structure of UDP-galactose-4-epimerase from Aspergillus nidulans
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0003978 | molecular_function | UDP-glucose 4-epimerase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006012 | biological_process | galactose metabolic process |
A | 0016853 | molecular_function | isomerase activity |
A | 0033499 | biological_process | galactose catabolic process via UDP-galactose |
B | 0000166 | molecular_function | nucleotide binding |
B | 0003978 | molecular_function | UDP-glucose 4-epimerase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006012 | biological_process | galactose metabolic process |
B | 0016853 | molecular_function | isomerase activity |
B | 0033499 | biological_process | galactose catabolic process via UDP-galactose |
C | 0000166 | molecular_function | nucleotide binding |
C | 0003978 | molecular_function | UDP-glucose 4-epimerase activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0006012 | biological_process | galactose metabolic process |
C | 0016853 | molecular_function | isomerase activity |
C | 0033499 | biological_process | galactose catabolic process via UDP-galactose |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE UPG A 401 |
Chain | Residue |
A | LYS88 |
A | LEU235 |
A | LEU236 |
A | VAL237 |
A | PHE238 |
A | ALA249 |
A | ARG251 |
A | TYR253 |
A | ARG313 |
A | ASP316 |
A | NAD402 |
A | SER128 |
A | ALA129 |
A | TYR156 |
A | PHE198 |
A | ASN199 |
A | ASN219 |
A | LEU220 |
A | LEU223 |
site_id | AC2 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE NAD A 402 |
Chain | Residue |
A | THR12 |
A | GLY13 |
A | TYR14 |
A | ILE15 |
A | ASP34 |
A | ASN35 |
A | TYR37 |
A | ASN38 |
A | SER39 |
A | LEU60 |
A | ASP61 |
A | VAL62 |
A | PHE84 |
A | ALA85 |
A | ALA86 |
A | LYS88 |
A | SER128 |
A | TYR156 |
A | LYS160 |
A | TYR197 |
A | PHE198 |
A | PRO200 |
A | UPG401 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL A 403 |
Chain | Residue |
A | GLU146 |
A | HIS147 |
A | ALA279 |
A | ARG326 |
site_id | AC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE IOD A 405 |
Chain | Residue |
A | ARG312 |
site_id | AC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE IOD A 406 |
Chain | Residue |
A | PRO97 |
A | GLN174 |
site_id | AC6 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE UDP B 401 |
Chain | Residue |
B | ASN199 |
B | ASN219 |
B | LEU220 |
B | LEU223 |
B | LEU236 |
B | VAL237 |
B | PHE238 |
B | ALA249 |
B | ARG251 |
B | VAL290 |
B | ARG313 |
B | ASP316 |
site_id | AC7 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE NAD B 402 |
Chain | Residue |
B | THR12 |
B | GLY13 |
B | TYR14 |
B | ILE15 |
B | ASP34 |
B | ASN35 |
B | TYR37 |
B | ASN38 |
B | SER39 |
B | LEU60 |
B | ASP61 |
B | VAL62 |
B | PHE84 |
B | ALA85 |
B | ALA86 |
B | LYS88 |
B | SER126 |
B | SER127 |
B | SER128 |
B | TYR156 |
B | LYS160 |
B | TYR197 |
B | PHE198 |
B | PRO200 |
B | HOH518 |
B | HOH522 |
site_id | AC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE IOD B 404 |
Chain | Residue |
B | ALA243 |
B | ARG312 |
site_id | AC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE IOD B 405 |
Chain | Residue |
B | GLN174 |
C | LEU98 |
site_id | BC1 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE UDP C 401 |
Chain | Residue |
C | PHE238 |
C | ARG251 |
C | VAL290 |
C | ARG313 |
C | ASP316 |
C | HOH502 |
C | ASN199 |
C | TYR218 |
C | ASN219 |
C | LEU220 |
C | LEU223 |
C | LEU235 |
C | LEU236 |
C | VAL237 |
site_id | BC2 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE NAD C 402 |
Chain | Residue |
C | THR12 |
C | GLY13 |
C | TYR14 |
C | ILE15 |
C | ASP34 |
C | ASN35 |
C | TYR37 |
C | ASN38 |
C | SER39 |
C | LEU60 |
C | ASP61 |
C | VAL62 |
C | PHE84 |
C | ALA85 |
C | ALA86 |
C | LYS88 |
C | SER126 |
C | SER127 |
C | SER128 |
C | TYR156 |
C | LYS160 |
C | TYR197 |
C | PRO200 |
C | HOH511 |
C | HOH515 |
site_id | BC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE IOD C 404 |
Chain | Residue |
C | ALA243 |
C | ARG312 |
site_id | BC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE IOD C 405 |
Chain | Residue |
B | PRO97 |
C | GLN174 |