1DLJ
THE FIRST STRUCTURE OF UDP-GLUCOSE DEHYDROGENASE (UDPGDH) REVEALS THE CATALYTIC RESIDUES NECESSARY FOR THE TWO-FOLD OXIDATION
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000271 | biological_process | polysaccharide biosynthetic process |
A | 0003979 | molecular_function | UDP-glucose 6-dehydrogenase activity |
A | 0006065 | biological_process | UDP-glucuronate biosynthetic process |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
A | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 A 405 |
Chain | Residue |
A | ARG144 |
A | HOH622 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 406 |
Chain | Residue |
A | VAL364 |
A | ASN365 |
A | ASP366 |
A | HOH667 |
A | HOH681 |
A | HOH787 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 407 |
Chain | Residue |
A | LYS332 |
A | GOL409 |
A | HOH504 |
A | HOH518 |
A | GLU328 |
site_id | AC4 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE NAI A 403 |
Chain | Residue |
A | GLY7 |
A | GLY9 |
A | TYR10 |
A | VAL11 |
A | VAL28 |
A | ASP29 |
A | ILE30 |
A | LEU31 |
A | LYS34 |
A | ALA80 |
A | THR81 |
A | PRO82 |
A | THR83 |
A | THR99 |
A | SER117 |
A | THR118 |
A | GLU141 |
A | LEU143 |
A | GLU145 |
A | TYR259 |
A | LYS263 |
A | ARG327 |
A | UGA404 |
A | GOL409 |
A | HOH440 |
A | HOH492 |
A | HOH531 |
A | HOH608 |
site_id | AC5 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE UGA A 404 |
Chain | Residue |
A | GLU141 |
A | PHE142 |
A | LEU143 |
A | ARG144 |
A | GLU145 |
A | LYS204 |
A | ASN208 |
A | VAL215 |
A | ARG244 |
A | TYR249 |
A | ASN250 |
A | ASN251 |
A | SER253 |
A | GLY257 |
A | SER260 |
A | MET319 |
A | LYS320 |
A | ARG381 |
A | ASP402 |
A | NAI403 |
A | HOH411 |
A | HOH412 |
A | HOH413 |
A | HOH414 |
A | HOH425 |
A | HOH456 |
A | HOH465 |
site_id | AC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL A 408 |
Chain | Residue |
A | PRO276 |
A | GLN277 |
A | GLN277 |
A | HOH419 |
A | HOH461 |
A | HOH461 |
A | HOH478 |
A | HOH517 |
A | HOH559 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 409 |
Chain | Residue |
A | PRO82 |
A | ASN84 |
A | TYR259 |
A | ARG327 |
A | NAI403 |
A | SO4407 |
A | HOH518 |
site_id | AC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 410 |
Chain | Residue |
A | PHE142 |
A | ARG144 |
A | SER156 |
A | HOH445 |
A | HOH462 |
A | HOH579 |
A | HOH587 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:14686915 |
Chain | Residue | Details |
A | SER260 |
site_id | SWS_FT_FI2 |
Number of Residues | 13 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10841783 |
Chain | Residue | Details |
A | LYS2 | |
A | MET319 | |
A | LYS320 | |
A | ARG327 | |
A | ASP402 | |
A | ASP29 | |
A | LYS34 | |
A | THR83 | |
A | THR118 | |
A | GLU145 | |
A | LYS204 | |
A | GLY257 | |
A | LYS263 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10841783, ECO:0007744|PDB:1DLI |
Chain | Residue | Details |
A | PHE142 | |
A | TYR249 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1dli |
Chain | Residue | Details |
A | ASP264 | |
A | LYS204 | |
A | THR118 | |
A | ASN208 | |
A | GLU145 | |
A | SER260 |
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 92 |
Chain | Residue | Details |
A | THR118 | activator, electrostatic stabiliser, hydrogen bond acceptor |
A | GLU145 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | LYS204 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
A | ASN208 | electrostatic stabiliser, hydrogen bond donor |
A | SER260 | covalently attached, nucleofuge, nucleophile |
A | ASP264 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |