3UND
Substrate-bound crystal structure of 2-dehydro-3-deoxyphosphooctonate aldolase from Burkholderia pseudomallei
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008676 | molecular_function | 3-deoxy-8-phosphooctulonate synthase activity |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0019294 | biological_process | keto-3-deoxy-D-manno-octulosonic acid biosynthetic process |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0008676 | molecular_function | 3-deoxy-8-phosphooctulonate synthase activity |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0019294 | biological_process | keto-3-deoxy-D-manno-octulosonic acid biosynthetic process |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0008676 | molecular_function | 3-deoxy-8-phosphooctulonate synthase activity |
| C | 0009058 | biological_process | biosynthetic process |
| C | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| C | 0016740 | molecular_function | transferase activity |
| C | 0019294 | biological_process | keto-3-deoxy-D-manno-octulosonic acid biosynthetic process |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0008676 | molecular_function | 3-deoxy-8-phosphooctulonate synthase activity |
| D | 0009058 | biological_process | biosynthetic process |
| D | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| D | 0016740 | molecular_function | transferase activity |
| D | 0019294 | biological_process | keto-3-deoxy-D-manno-octulosonic acid biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE A5P A 301 |
| Chain | Residue |
| A | ASN24 |
| A | SER212 |
| A | ASP248 |
| A | EDO282 |
| A | PEP304 |
| A | HOH358 |
| A | HOH378 |
| C | ARG118 |
| A | LYS58 |
| A | ASN60 |
| A | ARG61 |
| A | SER62 |
| A | HIS200 |
| A | GLN203 |
| A | ARG205 |
| A | ALA211 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PEP A 304 |
| Chain | Residue |
| A | LYS53 |
| A | SER55 |
| A | LYS58 |
| A | ASP93 |
| A | GLN111 |
| A | PRO113 |
| A | ALA114 |
| A | LYS136 |
| A | ARG166 |
| A | HIS200 |
| A | PHE235 |
| A | EDO282 |
| A | HOH293 |
| A | A5P301 |
| A | HOH356 |
| A | HOH373 |
| site_id | AC3 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE KD0 A 306 |
| Chain | Residue |
| A | ASN24 |
| A | LYS53 |
| A | SER55 |
| A | LYS58 |
| A | ASN60 |
| A | ARG61 |
| A | SER62 |
| A | ASP93 |
| A | GLN111 |
| A | LYS136 |
| A | HIS200 |
| A | GLN203 |
| A | ARG205 |
| A | ALA211 |
| A | SER212 |
| A | PHE235 |
| A | ASP248 |
| A | EDO282 |
| A | HOH358 |
| A | HOH378 |
| C | ARG118 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 316 |
| Chain | Residue |
| A | ASN13 |
| A | ARG183 |
| A | VAL194 |
| A | GLY230 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE EDO A 282 |
| Chain | Residue |
| A | PHE115 |
| A | GLN139 |
| A | ARG166 |
| A | GLN203 |
| A | ARG205 |
| A | A5P301 |
| A | PEP304 |
| A | KD0306 |
| A | HOH373 |
| A | HOH767 |
| C | ARG118 |
| site_id | AC6 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE A5P B 301 |
| Chain | Residue |
| B | ASN24 |
| B | LYS58 |
| B | ASN60 |
| B | ARG61 |
| B | SER62 |
| B | HIS200 |
| B | GLN203 |
| B | ARG205 |
| B | ALA211 |
| B | SER212 |
| B | ASP248 |
| B | EDO282 |
| B | PEP304 |
| B | HOH311 |
| B | HOH621 |
| D | ARG118 |
| site_id | AC7 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE PEP B 304 |
| Chain | Residue |
| B | LYS53 |
| B | SER55 |
| B | LYS58 |
| B | ASP93 |
| B | GLN111 |
| B | PRO113 |
| B | ALA114 |
| B | LYS136 |
| B | ARG166 |
| B | HIS200 |
| B | PHE235 |
| B | A5P301 |
| B | HOH314 |
| B | HOH317 |
| B | HOH740 |
| site_id | AC8 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE KD0 B 306 |
| Chain | Residue |
| B | ASN24 |
| B | LYS53 |
| B | SER55 |
| B | LYS58 |
| B | ASN60 |
| B | ARG61 |
| B | SER62 |
| B | LYS136 |
| B | HIS200 |
| B | GLN203 |
| B | ARG205 |
| B | ALA211 |
| B | SER212 |
| B | PHE235 |
| B | GLU237 |
| B | CYS247 |
| B | ASP248 |
| B | EDO282 |
| B | HOH311 |
| B | HOH621 |
| D | ARG118 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 316 |
| Chain | Residue |
| B | ASN13 |
| B | PHE182 |
| B | VAL194 |
| B | GLY230 |
| site_id | BC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE EDO B 282 |
| Chain | Residue |
| B | PHE115 |
| B | GLN139 |
| B | ARG166 |
| B | GLN203 |
| B | ARG205 |
| B | A5P301 |
| B | KD0306 |
| B | HOH740 |
| B | HOH754 |
| B | HOH755 |
| D | ARG118 |
| site_id | BC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE A5P C 301 |
| Chain | Residue |
| A | ARG118 |
| C | ASN24 |
| C | LYS58 |
| C | ASN60 |
| C | ARG61 |
| C | SER62 |
| C | HIS200 |
| C | GLN203 |
| C | ARG205 |
| C | ALA211 |
| C | SER212 |
| C | ASP248 |
| C | EDO282 |
| C | PEP304 |
| C | HOH341 |
| C | HOH369 |
| site_id | BC3 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PEP C 304 |
| Chain | Residue |
| C | LYS53 |
| C | SER55 |
| C | LYS58 |
| C | ASP93 |
| C | GLN111 |
| C | PRO113 |
| C | ALA114 |
| C | LYS136 |
| C | ARG166 |
| C | HIS200 |
| C | PHE235 |
| C | EDO282 |
| C | HOH293 |
| C | A5P301 |
| C | HOH388 |
| C | HOH416 |
| site_id | BC4 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE KD0 C 306 |
| Chain | Residue |
| A | ARG118 |
| C | ASN24 |
| C | LYS53 |
| C | SER55 |
| C | LYS58 |
| C | ASN60 |
| C | ARG61 |
| C | SER62 |
| C | GLN111 |
| C | LYS136 |
| C | HIS200 |
| C | GLN203 |
| C | ARG205 |
| C | ALA211 |
| C | SER212 |
| C | PHE235 |
| C | ASP248 |
| C | EDO282 |
| C | HOH341 |
| C | HOH369 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO C 316 |
| Chain | Residue |
| C | ASN13 |
| C | VAL229 |
| C | GLY230 |
| C | ILE231 |
| site_id | BC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO C 282 |
| Chain | Residue |
| A | ARG118 |
| C | PHE115 |
| C | GLN139 |
| C | ARG166 |
| C | GLN203 |
| C | ARG205 |
| C | A5P301 |
| C | PEP304 |
| C | KD0306 |
| site_id | BC7 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE A5P D 301 |
| Chain | Residue |
| B | ARG118 |
| D | ASN24 |
| D | LYS58 |
| D | ASN60 |
| D | ARG61 |
| D | SER62 |
| D | HIS200 |
| D | GLN203 |
| D | ARG205 |
| D | ALA211 |
| D | SER212 |
| D | ASP248 |
| D | PEP304 |
| D | HOH606 |
| D | HOH733 |
| D | HOH762 |
| site_id | BC8 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PEP D 304 |
| Chain | Residue |
| D | LYS53 |
| D | SER55 |
| D | LYS58 |
| D | ASP93 |
| D | GLN111 |
| D | PRO113 |
| D | ALA114 |
| D | LYS136 |
| D | ARG166 |
| D | PHE235 |
| D | HOH294 |
| D | A5P301 |
| D | HOH305 |
| D | HOH322 |
| site_id | BC9 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE KD0 D 306 |
| Chain | Residue |
| B | ARG118 |
| D | ASN24 |
| D | LYS53 |
| D | SER55 |
| D | LYS58 |
| D | ASN60 |
| D | ARG61 |
| D | SER62 |
| D | GLN111 |
| D | LYS136 |
| D | HIS200 |
| D | GLN203 |
| D | ARG205 |
| D | ALA211 |
| D | SER212 |
| D | PHE235 |
| D | GLU237 |
| D | CYS247 |
| D | ASP248 |
| D | HOH606 |
| D | HOH733 |
| site_id | CC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO D 316 |
| Chain | Residue |
| D | ASN13 |
| D | PHE182 |
| D | VAL194 |
| D | GLY230 |
