1XEL
UDP-GALACTOSE 4-EPIMERASE FROM ESCHERICHIA COLI
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 352 |
| Chain | Residue |
| A | GLN91 |
| A | HOH392 |
| A | HOH393 |
| A | HOH534 |
| A | HOH616 |
| A | HOH749 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 353 |
| Chain | Residue |
| A | HOH546 |
| A | HOH596 |
| A | GLN334 |
| A | HOH542 |
| A | HOH545 |
| site_id | AC3 |
| Number of Residues | 31 |
| 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 | PRO180 |
| A | UPG341 |
| A | EDO351 |
| A | HOH355 |
| A | HOH379 |
| A | HOH382 |
| A | HOH411 |
| A | HOH514 |
| site_id | AC4 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE UPG A 341 |
| Chain | Residue |
| A | SER124 |
| A | THR126 |
| A | TYR149 |
| A | PHE178 |
| A | ASN179 |
| A | ASN198 |
| A | ASN199 |
| A | LEU200 |
| A | LEU215 |
| A | ALA216 |
| A | ILE217 |
| A | PHE218 |
| A | GLY229 |
| A | ARG231 |
| A | TYR233 |
| A | VAL269 |
| A | ARG292 |
| A | ASP295 |
| A | TYR299 |
| A | NAD340 |
| A | HOH414 |
| A | HOH428 |
| A | HOH499 |
| A | HOH501 |
| A | HOH527 |
| A | HOH549 |
| A | HOH570 |
| A | HOH597 |
| A | HOH724 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 351 |
| Chain | Residue |
| A | TYR11 |
| A | ASN35 |
| A | GLY190 |
| A | ASP192 |
| A | NAD340 |
| A | HOH356 |
| A | HOH421 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEG A 354 |
| Chain | Residue |
| A | LEU250 |
| A | LYS253 |
| A | TYR259 |
| A | GLU309 |
| A | HOH614 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| 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 | 14 |
| 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 | 11 |
| 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 | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | ASN100 | |
| A | THR126 | |
| A | TYR149 | |
| A | LYS153 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | GLN146 | |
| A | LYS153 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | TYR149 | |
| A | 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 |
