1LRJ
Crystal Structure of E. coli UDP-Galactose 4-Epimerase Complexed with UDP-N-Acetylglucosamine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003978 | molecular_function | UDP-glucose 4-epimerase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0006012 | biological_process | galactose metabolic process |
| A | 0009242 | biological_process | colanic acid biosynthetic process |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0016857 | molecular_function | racemase and epimerase activity, acting on carbohydrates and derivatives |
| A | 0033499 | biological_process | galactose catabolic process via UDP-galactose |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0070403 | molecular_function | NAD+ binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 343 |
| Chain | Residue |
| A | GLN334 |
| A | TYR336 |
| A | HOH481 |
| A | HOH566 |
| A | HOH622 |
| A | HOH683 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA A 344 |
| Chain | Residue |
| A | GLN91 |
| A | HOH536 |
| A | HOH757 |
| site_id | AC3 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE NAD A 340 |
| Chain | Residue |
| A | GLY7 |
| A | GLY10 |
| A | TYR11 |
| A | ILE12 |
| A | ASP31 |
| A | ASN32 |
| A | LEU33 |
| A | CYS34 |
| A | ASN35 |
| A | SER36 |
| A | GLY57 |
| A | ASP58 |
| A | ILE59 |
| A | PHE80 |
| A | ALA81 |
| A | GLY82 |
| A | LYS84 |
| A | ASN99 |
| A | SER122 |
| A | SER123 |
| A | TYR149 |
| A | LYS153 |
| A | TYR177 |
| A | PHE178 |
| A | PRO180 |
| A | ASN199 |
| A | UD1341 |
| A | HOH346 |
| A | HOH347 |
| A | HOH353 |
| A | HOH357 |
| A | HOH395 |
| A | HOH456 |
| A | HOH584 |
| A | HOH719 |
| site_id | AC4 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE UD1 A 341 |
| Chain | Residue |
| A | LYS84 |
| A | VAL86 |
| A | SER124 |
| A | THR126 |
| A | TYR177 |
| A | PHE178 |
| A | ASN179 |
| A | ASN199 |
| A | LEU200 |
| A | LEU215 |
| A | ALA216 |
| A | ILE217 |
| A | PHE218 |
| A | ARG231 |
| A | TYR233 |
| A | VAL269 |
| A | ARG292 |
| A | ASP295 |
| A | TYR299 |
| A | NAD340 |
| A | HOH393 |
| A | HOH404 |
| A | HOH710 |
| A | HOH719 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PGE A 342 |
| Chain | Residue |
| A | LEU250 |
| A | LYS253 |
| A | GLU309 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:8611497 |
| Chain | Residue | Details |
| A | TYR149 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 7 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12019271, ECO:0000269|PubMed:1579570, ECO:0000269|PubMed:8611497, ECO:0000269|PubMed:8611559, ECO:0000269|PubMed:8931134, ECO:0000269|PubMed:9174344, ECO:0000269|PubMed:9271498, ECO:0000269|PubMed:9271499, ECO:0000269|PubMed:9708982 |
| Chain | Residue | Details |
| A | TYR11 | |
| A | ASP31 | |
| A | ASP58 | |
| A | PHE80 | |
| A | ASN99 | |
| A | LYS153 | |
| A | PHE178 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | SER124 | |
| A | TYR149 | |
| A | ASN179 | |
| A | ASN199 | |
| A | ALA216 | |
| A | ARG231 | |
| A | ARG292 | |
| A | TYR299 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 188 |
| Chain | Residue | Details |
| A | SER124 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | TYR149 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | LYS153 | activator, hydrogen bond donor |
