2C20
CRYSTAL STRUCTURE OF UDP-GLUCOSE 4-EPIMERASE
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 | 0006012 | biological_process | galactose metabolic process |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0033499 | biological_process | galactose catabolic process via UDP-galactose, Leloir pathway |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003978 | molecular_function | UDP-glucose 4-epimerase activity |
| B | 0006012 | biological_process | galactose metabolic process |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0033499 | biological_process | galactose catabolic process via UDP-galactose, Leloir pathway |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0003978 | molecular_function | UDP-glucose 4-epimerase activity |
| C | 0006012 | biological_process | galactose metabolic process |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0033499 | biological_process | galactose catabolic process via UDP-galactose, Leloir pathway |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0003978 | molecular_function | UDP-glucose 4-epimerase activity |
| D | 0006012 | biological_process | galactose metabolic process |
| D | 0016853 | molecular_function | isomerase activity |
| D | 0033499 | biological_process | galactose catabolic process via UDP-galactose, Leloir pathway |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0003978 | molecular_function | UDP-glucose 4-epimerase activity |
| E | 0006012 | biological_process | galactose metabolic process |
| E | 0016853 | molecular_function | isomerase activity |
| E | 0033499 | biological_process | galactose catabolic process via UDP-galactose, Leloir pathway |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0003978 | molecular_function | UDP-glucose 4-epimerase activity |
| F | 0006012 | biological_process | galactose metabolic process |
| F | 0016853 | molecular_function | isomerase activity |
| F | 0033499 | biological_process | galactose catabolic process via UDP-galactose, Leloir pathway |
| F | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 601 |
| Chain | Residue |
| A | GLU183 |
| A | HIS185 |
| A | GLU188 |
| A | HIS190 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 601 |
| Chain | Residue |
| B | GLU183 |
| B | HIS185 |
| B | GLU188 |
| B | HIS190 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 601 |
| Chain | Residue |
| C | HIS185 |
| C | GLU188 |
| C | HIS190 |
| C | GLU183 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 601 |
| Chain | Residue |
| D | GLU183 |
| D | HIS185 |
| D | GLU188 |
| D | HIS190 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN E 601 |
| Chain | Residue |
| E | GLU183 |
| E | HIS185 |
| E | GLU188 |
| E | HIS190 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN F 601 |
| Chain | Residue |
| F | GLU183 |
| F | HIS185 |
| F | GLU188 |
| F | HIS190 |
| site_id | AC7 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAD A 401 |
| Chain | Residue |
| A | GLY8 |
| A | ALA10 |
| A | GLY11 |
| A | TYR12 |
| A | ILE13 |
| A | ASP32 |
| A | ASN33 |
| A | GLN35 |
| A | THR36 |
| A | GLY37 |
| A | GLY51 |
| A | ASP52 |
| A | LEU53 |
| A | PHE74 |
| A | ALA75 |
| A | ALA76 |
| A | ASN93 |
| A | SER116 |
| A | SER117 |
| A | TYR142 |
| A | LYS146 |
| A | TYR169 |
| A | PHE170 |
| A | VAL172 |
| A | HIS185 |
| A | HIS190 |
| A | HOH2040 |
| A | HOH2041 |
| site_id | AC8 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NAD B 401 |
| Chain | Residue |
| B | GLY8 |
| B | ALA10 |
| B | GLY11 |
| B | TYR12 |
| B | ILE13 |
| B | ASP32 |
| B | ASN33 |
| B | GLN35 |
| B | THR36 |
| B | GLY37 |
| B | GLY51 |
| B | ASP52 |
| B | LEU53 |
| B | PHE74 |
| B | ALA75 |
| B | ALA76 |
| B | SER78 |
| B | ASN93 |
| B | SER117 |
| B | THR118 |
| B | TYR142 |
| B | LYS146 |
| B | TYR169 |
| B | PHE170 |
| B | ASN171 |
| B | VAL172 |
| B | HIS185 |
| B | HOH2005 |
| B | HOH2041 |
| site_id | AC9 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NAD C 401 |
| Chain | Residue |
| C | ASN93 |
| C | SER116 |
| C | SER117 |
| C | TYR142 |
| C | LYS146 |
| C | TYR169 |
| C | PHE170 |
| C | VAL172 |
| C | HIS185 |
| C | HOH2031 |
| C | HOH2038 |
| C | GLY8 |
| C | ALA10 |
| C | GLY11 |
| C | TYR12 |
| C | ILE13 |
| C | ASP32 |
| C | ASN33 |
| C | LEU34 |
| C | GLN35 |
| C | THR36 |
| C | GLY37 |
| C | GLY51 |
| C | ASP52 |
| C | LEU53 |
| C | PHE74 |
| C | ALA75 |
| C | ALA76 |
| C | SER78 |
| site_id | BC1 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NAD D 401 |
| Chain | Residue |
| D | GLY8 |
| D | ALA10 |
| D | GLY11 |
| D | TYR12 |
| D | ILE13 |
| D | ASP32 |
| D | ASN33 |
| D | LEU34 |
| D | GLN35 |
| D | THR36 |
| D | GLY37 |
| D | GLY51 |
| D | ASP52 |
| D | LEU53 |
| D | PHE74 |
| D | ALA75 |
| D | ALA76 |
| D | SER78 |
| D | ASN93 |
| D | SER117 |
| D | THR118 |
| D | TYR142 |
| D | LYS146 |
| D | TYR169 |
| D | PHE170 |
| D | ASN171 |
| D | VAL172 |
| D | HIS185 |
| D | HIS190 |
| D | HOH2031 |
| D | HOH2036 |
| site_id | BC2 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAD E 401 |
| Chain | Residue |
| E | GLY8 |
| E | ALA10 |
| E | GLY11 |
| E | TYR12 |
| E | ILE13 |
| E | ASP32 |
| E | ASN33 |
| E | GLN35 |
| E | THR36 |
| E | GLY37 |
| E | GLY51 |
| E | ASP52 |
| E | LEU53 |
| E | PHE74 |
| E | ALA75 |
| E | ALA76 |
| E | SER78 |
| E | ASN93 |
| E | SER117 |
| E | TYR142 |
| E | LYS146 |
| E | TYR169 |
| E | PHE170 |
| E | VAL172 |
| E | HIS185 |
| E | HIS190 |
| E | HOH2005 |
| E | HOH2031 |
| site_id | BC3 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NAD F 401 |
| Chain | Residue |
| F | GLY8 |
| F | ALA10 |
| F | GLY11 |
| F | TYR12 |
| F | ILE13 |
| F | ASP32 |
| F | ASN33 |
| F | GLN35 |
| F | THR36 |
| F | GLY37 |
| F | GLY51 |
| F | ASP52 |
| F | LEU53 |
| F | PHE74 |
| F | ALA75 |
| F | ALA76 |
| F | SER78 |
| F | ASN93 |
| F | SER117 |
| F | THR118 |
| F | TYR142 |
| F | LYS146 |
| F | TYR169 |
| F | PHE170 |
| F | ASN171 |
| F | VAL172 |
| F | HIS185 |
| F | HOH2035 |
| F | HOH2042 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| A | TYR142 | |
| A | THR118 | |
| A | ALA120 | |
| A | LYS146 |
| site_id | CSA10 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| D | THR118 | |
| D | TYR142 | |
| D | LYS146 |
| site_id | CSA11 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| E | THR118 | |
| E | TYR142 | |
| E | LYS146 |
| site_id | CSA12 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| F | THR118 | |
| F | TYR142 | |
| F | LYS146 |
| site_id | CSA13 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| A | TYR142 | |
| A | SER116 | |
| A | ASN94 | |
| A | LYS146 |
| site_id | CSA14 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| B | TYR142 | |
| B | SER116 | |
| B | ASN94 | |
| B | LYS146 |
| site_id | CSA15 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| C | TYR142 | |
| C | SER116 | |
| C | ASN94 | |
| C | LYS146 |
| site_id | CSA16 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| D | TYR142 | |
| D | SER116 | |
| D | ASN94 | |
| D | LYS146 |
| site_id | CSA17 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| E | TYR142 | |
| E | SER116 | |
| E | ASN94 | |
| E | LYS146 |
| site_id | CSA18 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| F | TYR142 | |
| F | SER116 | |
| F | ASN94 | |
| F | LYS146 |
| site_id | CSA19 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| A | TYR142 | |
| A | LYS146 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| B | TYR142 | |
| B | THR118 | |
| B | ALA120 | |
| B | LYS146 |
| site_id | CSA20 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| B | TYR142 | |
| B | LYS146 |
| site_id | CSA21 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| C | TYR142 | |
| C | LYS146 |
| site_id | CSA22 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| D | TYR142 | |
| D | LYS146 |
| site_id | CSA23 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| E | TYR142 | |
| E | LYS146 |
| site_id | CSA24 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| F | TYR142 | |
| F | LYS146 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| C | TYR142 | |
| C | THR118 | |
| C | ALA120 | |
| C | LYS146 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| D | TYR142 | |
| D | THR118 | |
| D | ALA120 | |
| D | LYS146 |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| E | TYR142 | |
| E | THR118 | |
| E | ALA120 | |
| E | LYS146 |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| F | TYR142 | |
| F | THR118 | |
| F | ALA120 | |
| F | LYS146 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| A | THR118 | |
| A | TYR142 | |
| A | LYS146 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| B | THR118 | |
| B | TYR142 | |
| B | LYS146 |
| site_id | CSA9 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| C | THR118 | |
| C | TYR142 | |
| C | LYS146 |
