5GY7
X-Ray structure of H243I mutant of UDP-Galactose 4-epimerase from E.coli:evidence for existence of open and closed active site during catalysis.
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 |
| 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 | 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 |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0070403 | molecular_function | NAD+ binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | binding site for residue UDP A 401 |
| Chain | Residue |
| A | ASN179 |
| A | VAL269 |
| A | ARG292 |
| A | ASP295 |
| A | HOH554 |
| A | HOH577 |
| A | HOH598 |
| A | HOH658 |
| A | HOH674 |
| A | HOH682 |
| A | HOH757 |
| A | ASN198 |
| A | ASN199 |
| A | LEU200 |
| A | ALA216 |
| A | ILE217 |
| A | PHE218 |
| A | ARG231 |
| A | TYR233 |
| site_id | AC2 |
| Number of Residues | 32 |
| Details | binding site for residue NAD A 402 |
| 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 | HOH523 |
| A | HOH547 |
| A | HOH559 |
| A | HOH592 |
| A | HOH595 |
| A | HOH638 |
| A | HOH650 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | binding site for residue GOL A 403 |
| Chain | Residue |
| A | ARG331 |
| A | HIS332 |
| A | HOH513 |
| A | HOH542 |
| A | HOH720 |
| B | ASN267 |
| B | THR317 |
| B | LEU318 |
| B | ASP319 |
| site_id | AC4 |
| Number of Residues | 20 |
| Details | binding site for residue UDP B 401 |
| Chain | Residue |
| B | ASN179 |
| B | ASN198 |
| B | ASN199 |
| B | LEU200 |
| B | ALA216 |
| B | ILE217 |
| B | PHE218 |
| B | ARG231 |
| B | TYR233 |
| B | VAL269 |
| B | ARG292 |
| B | ASP295 |
| B | HOH548 |
| B | HOH551 |
| B | HOH599 |
| B | HOH640 |
| B | HOH656 |
| B | HOH665 |
| B | HOH702 |
| B | HOH713 |
| site_id | AC5 |
| Number of Residues | 33 |
| Details | binding site for residue NAD B 402 |
| Chain | Residue |
| B | SER123 |
| B | TYR149 |
| B | LYS153 |
| B | TYR177 |
| B | PHE178 |
| B | PRO180 |
| B | HOH519 |
| B | HOH555 |
| B | HOH579 |
| B | HOH582 |
| B | HOH593 |
| B | HOH615 |
| B | HOH626 |
| B | HOH632 |
| 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 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue NO3 B 403 |
| Chain | Residue |
| B | ARG38 |
| B | PRO223 |
| B | ARG291 |
| B | PRO297 |
| B | HOH561 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:8611497 |
| Chain | Residue | Details |
| A | TYR149 | |
| B | TYR149 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| 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 | |
| B | ASP58 | |
| B | PHE80 | |
| B | ASN99 | |
| B | LYS153 | |
| B | PHE178 | |
| A | ASP31 | |
| A | ASP58 | |
| A | PHE80 | |
| A | ASN99 | |
| A | LYS153 | |
| A | PHE178 | |
| B | TYR11 | |
| B | ASP31 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | SER124 | |
| B | TYR149 | |
| B | ASN179 | |
| B | ASN199 | |
| B | ALA216 | |
| B | ARG231 | |
| B | ARG292 | |
| B | TYR299 | |
| A | TYR149 | |
| A | ASN179 | |
| A | ASN199 | |
| A | ALA216 | |
| A | ARG231 | |
| A | ARG292 | |
| A | TYR299 | |
| B | SER124 |
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 |
| 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 |
