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 | 0005996 | biological_process | monosaccharide 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, Leloir pathway |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0070403 | molecular_function | NAD+ binding |
| B | 0003978 | molecular_function | UDP-glucose 4-epimerase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0005996 | biological_process | monosaccharide metabolic process |
| B | 0006012 | biological_process | galactose metabolic process |
| B | 0009242 | biological_process | colanic acid biosynthetic process |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0016857 | molecular_function | racemase and epimerase activity, acting on carbohydrates and derivatives |
| B | 0033499 | biological_process | galactose catabolic process via UDP-galactose, Leloir pathway |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0070403 | molecular_function | NAD+ binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B 411 |
| Chain | Residue |
| A | GLN91 |
| A | HOH440 |
| A | HOH441 |
| A | HOH616 |
| A | HOH694 |
| B | HOH413 |
| site_id | AC2 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NAD A 340 |
| Chain | Residue |
| 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 | SER124 |
| A | TYR149 |
| A | LYS153 |
| A | TYR177 |
| A | PHE178 |
| A | UPP341 |
| A | HOH352 |
| A | HOH368 |
| A | HOH420 |
| A | HOH422 |
| A | GLY7 |
| A | GLY10 |
| A | TYR11 |
| site_id | AC3 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE UPP A 341 |
| Chain | Residue |
| A | LYS84 |
| A | TYR149 |
| A | ASN179 |
| A | ASN198 |
| A | ASN199 |
| A | LEU200 |
| A | ALA216 |
| A | ILE217 |
| A | PHE218 |
| A | GLY229 |
| A | ARG231 |
| A | TYR233 |
| A | VAL269 |
| A | ARG292 |
| A | ASP295 |
| A | NAD340 |
| A | HOH427 |
| A | HOH429 |
| A | HOH492 |
| A | HOH494 |
| A | HOH511 |
| A | HOH550 |
| A | HOH551 |
| site_id | AC4 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NAD B 340 |
| Chain | Residue |
| B | GLY7 |
| B | GLY10 |
| B | TYR11 |
| B | ILE12 |
| B | ASP31 |
| B | ASN32 |
| B | LEU33 |
| B | CYS34 |
| B | ASN35 |
| B | SER36 |
| B | GLY57 |
| B | ASP58 |
| B | ILE59 |
| B | PHE80 |
| B | ALA81 |
| B | GLY82 |
| B | LYS84 |
| B | ASN99 |
| B | SER122 |
| B | SER123 |
| B | SER124 |
| B | TYR149 |
| B | LYS153 |
| B | TYR177 |
| B | PHE178 |
| B | UPP341 |
| B | HOH435 |
| B | HOH436 |
| B | HOH494 |
| B | HOH496 |
| B | HOH521 |
| B | HOH609 |
| B | HOH726 |
| site_id | AC5 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE UPP B 341 |
| Chain | Residue |
| B | ILE217 |
| B | PHE218 |
| B | GLY229 |
| B | ARG231 |
| B | TYR233 |
| B | ARG292 |
| B | ASP295 |
| B | TYR299 |
| B | NAD340 |
| B | HOH497 |
| B | HOH553 |
| B | HOH583 |
| B | HOH595 |
| B | HOH663 |
| B | HOH672 |
| B | VAL86 |
| B | ASN179 |
| B | ASN198 |
| B | ASN199 |
| B | LEU200 |
| B | LEU215 |
| B | ALA216 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 410 |
| Chain | Residue |
| A | ALA208 |
| B | THR315 |
| B | GLU320 |
| B | HOH678 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"8611497","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 28 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12019271","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1579570","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8611497","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8611559","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8931134","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9174344","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9271498","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9271499","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9708982","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 22 |
| Details | Binding site: {} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | TYR149 | |
| A | SER124 | |
| A | LYS153 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | TYR149 | |
| B | SER124 | |
| B | LYS153 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | ASN100 | |
| A | THR126 | |
| A | TYR149 | |
| A | LYS153 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | ASN100 | |
| B | THR126 | |
| B | TYR149 | |
| B | LYS153 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | GLN146 | |
| A | LYS153 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | GLN146 | |
| B | LYS153 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | TYR149 | |
| A | LYS153 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | TYR149 | |
| B | LYS153 |
| 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 |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 188 |
| Chain | Residue | Details |
| B | SER124 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| B | TYR149 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | LYS153 | activator, hydrogen bond donor |
