1DLI
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 | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 405 |
| Chain | Residue |
| A | ARG144 |
| A | LYS147 |
| A | GLU306 |
| A | HOH638 |
| A | HOH655 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 406 |
| Chain | Residue |
| A | HOH581 |
| A | HOH640 |
| A | LYS68 |
| A | VAL364 |
| A | ASN365 |
| A | ASP366 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 407 |
| Chain | Residue |
| A | GLU328 |
| A | LYS332 |
| A | GOL409 |
| A | HOH577 |
| A | HOH599 |
| site_id | AC4 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAD A 403 |
| Chain | Residue |
| A | GLY9 |
| A | TYR10 |
| A | VAL11 |
| 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 | CYS260 |
| A | LYS263 |
| A | ARG327 |
| A | UDX404 |
| A | GOL409 |
| A | HOH411 |
| A | HOH415 |
| A | HOH432 |
| A | HOH496 |
| A | HOH582 |
| site_id | AC5 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE UDX A 404 |
| Chain | Residue |
| A | GLU141 |
| A | PHE142 |
| A | LEU143 |
| A | ARG144 |
| A | GLU145 |
| A | LYS204 |
| A | VAL215 |
| A | ARG244 |
| A | TYR249 |
| A | ASN250 |
| A | ASN251 |
| A | SER253 |
| A | TYR256 |
| A | GLY257 |
| A | CYS260 |
| A | LEU261 |
| A | MET319 |
| A | LYS320 |
| A | ARG381 |
| A | ASP402 |
| A | NAD403 |
| A | HOH412 |
| A | HOH413 |
| A | HOH414 |
| A | HOH453 |
| A | HOH454 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 408 |
| Chain | Residue |
| A | PRO276 |
| A | GLN277 |
| A | GLN277 |
| A | GLU281 |
| A | HOH433 |
| A | HOH488 |
| A | HOH488 |
| A | HOH560 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 409 |
| Chain | Residue |
| A | PRO82 |
| A | ASN84 |
| A | TYR259 |
| A | ARG327 |
| A | NAD403 |
| A | SO4407 |
| A | HOH582 |
| A | HOH625 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 410 |
| Chain | Residue |
| A | PHE142 |
| A | ARG144 |
| A | PRO155 |
| A | SER156 |
| A | ARG244 |
| A | HOH435 |
| A | HOH479 |
| A | HOH627 |
| A | HOH638 |
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 | CYS260 |
| 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 | 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 | CYS260 | covalently attached, nucleofuge, nucleophile |
| A | ASP264 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
