3GG2
Crystal structure of UDP-glucose 6-dehydrogenase from Porphyromonas gingivalis bound to product UDP-glucuronate
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 | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| A | 0051287 | molecular_function | NAD binding |
| B | 0000271 | biological_process | polysaccharide biosynthetic process |
| B | 0003979 | molecular_function | UDP-glucose 6-dehydrogenase activity |
| B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| B | 0051287 | molecular_function | NAD binding |
| C | 0000271 | biological_process | polysaccharide biosynthetic process |
| C | 0003979 | molecular_function | UDP-glucose 6-dehydrogenase activity |
| C | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| C | 0051287 | molecular_function | NAD binding |
| D | 0000271 | biological_process | polysaccharide biosynthetic process |
| D | 0003979 | molecular_function | UDP-glucose 6-dehydrogenase activity |
| D | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| D | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE UGA A 1000 |
| Chain | Residue |
| A | HOH53 |
| A | ILE299 |
| A | PHE333 |
| A | LEU334 |
| A | TYR335 |
| A | GLY339 |
| A | TYR340 |
| A | GLY341 |
| A | CYS344 |
| A | PHE345 |
| A | PHE404 |
| A | TYR88 |
| A | LYS405 |
| A | ARG495 |
| A | HOH527 |
| A | HOH564 |
| A | HOH579 |
| A | HOH605 |
| A | HOH634 |
| A | HOH1795 |
| B | ARG328 |
| D | UGA5000 |
| A | GLU232 |
| A | PHE233 |
| A | LEU234 |
| A | LYS235 |
| A | GLU236 |
| A | LYS288 |
| A | ASN292 |
| site_id | AC2 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE UGA A 6000 |
| Chain | Residue |
| A | MET244 |
| A | LYS245 |
| A | MET269 |
| A | LEU270 |
| A | LEU271 |
| A | ASN272 |
| A | ARG275 |
| A | HOH536 |
| A | HOH542 |
| A | HOH574 |
| A | HOH577 |
| A | HOH814 |
| A | HOH1652 |
| D | PHE333 |
| D | TYR335 |
| D | LYS405 |
| D | PRO406 |
| D | GLU470 |
| D | HOH558 |
| D | UGA4000 |
| site_id | AC3 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE UGA B 2000 |
| Chain | Residue |
| A | ARG328 |
| B | HOH26 |
| B | TYR88 |
| B | GLU232 |
| B | PHE233 |
| B | LEU234 |
| B | LYS235 |
| B | GLU236 |
| B | LYS288 |
| B | ASN292 |
| B | ILE299 |
| B | PHE333 |
| B | LEU334 |
| B | TYR335 |
| B | TYR340 |
| B | GLY341 |
| B | CYS344 |
| B | PHE345 |
| B | PHE404 |
| B | LYS405 |
| B | ARG495 |
| B | HOH551 |
| B | HOH579 |
| B | HOH597 |
| B | HOH602 |
| B | HOH678 |
| B | HOH1098 |
| B | HOH1116 |
| B | HOH2215 |
| site_id | AC4 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE UGA C 3000 |
| Chain | Residue |
| C | HOH551 |
| C | HOH568 |
| C | HOH1112 |
| D | ARG328 |
| C | TYR88 |
| C | GLU232 |
| C | PHE233 |
| C | LEU234 |
| C | LYS235 |
| C | GLU236 |
| C | LYS288 |
| C | ASN292 |
| C | ILE299 |
| C | PHE333 |
| C | LEU334 |
| C | TYR335 |
| C | TYR340 |
| C | GLY341 |
| C | CYS344 |
| C | PHE345 |
| C | PHE404 |
| C | LYS405 |
| C | ARG495 |
| C | HOH529 |
| C | HOH537 |
| site_id | AC5 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE UGA D 4000 |
| Chain | Residue |
| A | UGA6000 |
| C | ARG328 |
| D | HOH45 |
| D | GLU232 |
| D | PHE233 |
| D | LEU234 |
| D | LYS235 |
| D | GLU236 |
| D | LYS288 |
| D | ASN292 |
| D | ILE299 |
| D | PHE333 |
| D | LEU334 |
| D | TYR335 |
| D | GLY339 |
| D | TYR340 |
| D | GLY341 |
| D | CYS344 |
| D | PHE345 |
| D | PHE404 |
| D | LYS405 |
| D | ARG495 |
| D | HOH533 |
| D | HOH1627 |
| D | HOH1636 |
| D | HOH1637 |
| D | HOH1638 |
| D | HOH1670 |
| site_id | AC6 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE UGA D 5000 |
| Chain | Residue |
| A | PHE333 |
| A | TYR335 |
| A | LYS405 |
| A | PRO406 |
| A | GLU470 |
| A | LYS472 |
| A | UGA1000 |
| A | HOH1657 |
| D | MET244 |
| D | LYS245 |
| D | MET269 |
| D | LEU270 |
| D | LEU271 |
| D | ASN272 |
| D | ARG275 |
| D | HOH536 |
| D | HOH549 |
| D | HOH1663 |
| D | HOH1664 |
| D | HOH1687 |
| D | HOH1699 |
| D | HOH1726 |
| D | HOH1772 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1dli |
| Chain | Residue | Details |
| A | THR199 | |
| A | ASP348 | |
| A | GLU236 | |
| A | ASN292 | |
| A | CYS344 | |
| A | LYS288 |
| site_id | CSA2 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1dli |
| Chain | Residue | Details |
| B | THR199 | |
| B | ASP348 | |
| B | GLU236 | |
| B | ASN292 | |
| B | CYS344 | |
| B | LYS288 |
| site_id | CSA3 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1dli |
| Chain | Residue | Details |
| C | THR199 | |
| C | ASP348 | |
| C | GLU236 | |
| C | ASN292 | |
| C | CYS344 | |
| C | LYS288 |
| site_id | CSA4 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1dli |
| Chain | Residue | Details |
| D | THR199 | |
| D | ASP348 | |
| D | GLU236 | |
| D | ASN292 | |
| D | CYS344 | |
| D | LYS288 |
