1UDB
STRUCTURE OF UDP-GALACTOSE-4-EPIMERASE COMPLEXED WITH UDP-4-DEOXY-4-FLUORO-ALPHA-D-GLUCOSE
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 412 |
| Chain | Residue |
| A | GLN91 |
| A | HOH510 |
| A | HOH564 |
| A | HOH627 |
| A | HOH656 |
| A | HOH723 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 413 |
| Chain | Residue |
| A | HOH793 |
| A | HOH985 |
| A | GLN194 |
| A | HOH551 |
| A | HOH679 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE NA A 414 |
| Chain | Residue |
| A | GLN334 |
| A | HOH632 |
| A | HOH640 |
| A | HOH838 |
| A | HOH889 |
| A | HOH961 |
| A | HOH1016 |
| site_id | AC4 |
| Number of Residues | 33 |
| 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 | UFG341 |
| A | EDO411 |
| A | HOH504 |
| A | HOH505 |
| A | HOH517 |
| A | HOH523 |
| A | HOH600 |
| A | HOH670 |
| A | HOH1020 |
| site_id | AC5 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE UFG A 341 |
| Chain | Residue |
| A | VAL86 |
| A | SER124 |
| A | THR126 |
| A | TYR149 |
| A | PHE178 |
| A | ASN179 |
| A | ASN198 |
| A | ASN199 |
| A | LEU200 |
| A | ALA216 |
| A | ILE217 |
| A | PHE218 |
| A | ARG231 |
| A | TYR233 |
| A | ARG292 |
| A | ASP295 |
| A | TYR299 |
| A | NAD340 |
| A | HOH518 |
| A | HOH563 |
| A | HOH581 |
| A | HOH613 |
| A | HOH642 |
| A | HOH659 |
| A | HOH663 |
| A | HOH668 |
| A | HOH670 |
| A | HOH672 |
| A | HOH691 |
| A | HOH698 |
| A | HOH952 |
| A | HOH1020 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 411 |
| Chain | Residue |
| A | TYR11 |
| A | ASN35 |
| A | ASP192 |
| A | NAD340 |
| A | HOH532 |
| A | HOH576 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEG A 410 |
| Chain | Residue |
| A | LEU250 |
| A | LYS253 |
| A | GLU309 |
| A | HOH634 |
| A | HOH916 |
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 | 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 |
