2PZM
Crystal structure of the Bordetella bronchiseptica enzyme WbmG in complex with NAD and UDP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0006541 | biological_process | glutamine metabolic process |
| A | 0008460 | molecular_function | dTDP-glucose 4,6-dehydratase activity |
| A | 0010253 | biological_process | UDP-rhamnose biosynthetic process |
| A | 0010280 | molecular_function | UDP-L-rhamnose synthase activity |
| A | 0010315 | biological_process | auxin export across the plasma membrane |
| A | 0016740 | molecular_function | transferase activity |
| A | 0050377 | molecular_function | UDP-glucose 4,6-dehydratase activity |
| A | 0051555 | biological_process | flavonol biosynthetic process |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0006541 | biological_process | glutamine metabolic process |
| B | 0008460 | molecular_function | dTDP-glucose 4,6-dehydratase activity |
| B | 0010253 | biological_process | UDP-rhamnose biosynthetic process |
| B | 0010280 | molecular_function | UDP-L-rhamnose synthase activity |
| B | 0010315 | biological_process | auxin export across the plasma membrane |
| B | 0016740 | molecular_function | transferase activity |
| B | 0050377 | molecular_function | UDP-glucose 4,6-dehydratase activity |
| B | 0051555 | biological_process | flavonol biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 701 |
| Chain | Residue |
| A | TYR79 |
| A | TYR140 |
| A | NAD601 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 702 |
| Chain | Residue |
| A | HIS229 |
| A | ASP281 |
| A | PHE282 |
| A | HOH842 |
| A | HOH893 |
| A | HOH926 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 703 |
| Chain | Residue |
| B | HIS229 |
| B | ASP281 |
| B | PHE282 |
| B | HOH743 |
| B | HOH784 |
| site_id | AC4 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE NAD A 601 |
| Chain | Residue |
| A | GLY7 |
| A | ALA9 |
| A | GLY10 |
| A | CYS11 |
| A | LEU12 |
| A | ASP31 |
| A | ASN32 |
| A | PHE33 |
| A | ALA34 |
| A | THR35 |
| A | GLY36 |
| A | GLY52 |
| A | SER53 |
| A | VAL54 |
| A | SER75 |
| A | ALA76 |
| A | ALA77 |
| A | TYR79 |
| A | THR91 |
| A | PHE114 |
| A | GLN115 |
| A | THR116 |
| A | TYR140 |
| A | LYS144 |
| A | ALA164 |
| A | ASN165 |
| A | VAL166 |
| A | SO4701 |
| A | HOH750 |
| A | HOH752 |
| A | HOH759 |
| A | HOH796 |
| A | HOH797 |
| A | HOH809 |
| site_id | AC5 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE NAD B 601 |
| Chain | Residue |
| B | GLY7 |
| B | ALA9 |
| B | GLY10 |
| B | CYS11 |
| B | LEU12 |
| B | ASP31 |
| B | ASN32 |
| B | PHE33 |
| B | ALA34 |
| B | THR35 |
| B | GLY36 |
| B | GLY52 |
| B | SER53 |
| B | VAL54 |
| B | SER75 |
| B | ALA76 |
| B | ALA77 |
| B | TYR79 |
| B | THR91 |
| B | PHE114 |
| B | GLN115 |
| B | THR116 |
| B | TYR140 |
| B | LYS144 |
| B | LEU163 |
| B | ALA164 |
| B | ASN165 |
| B | VAL166 |
| B | HOH713 |
| B | HOH758 |
| B | HOH805 |
| B | HOH809 |
| B | HOH810 |
| B | HOH825 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE UDP A 602 |
| Chain | Residue |
| A | THR178 |
| A | PHE190 |
| A | CYS191 |
| A | SER192 |
| A | THR194 |
| A | ARG196 |
| A | ILE231 |
| A | ASP259 |
| A | HOH780 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE UDP B 602 |
| Chain | Residue |
| B | THR178 |
| B | PHE190 |
| B | CYS191 |
| B | SER192 |
| B | ILE231 |
