2QKF
Crystal structure of 3-deoxy-d-manno-octulosonate 8-phosphate synthase (KDO8PS) from Neisseria meningitidis
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
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 | 0005829 | cellular_component | cytosol |
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 | 0005829 | cellular_component | cytosol |
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 | 0005829 | cellular_component | cytosol |
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 | 3 |
Details | BINDING SITE FOR RESIDUE CL B 281 |
Chain | Residue |
B | GLN138 |
B | ARG165 |
D | ARG117 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL C 281 |
Chain | Residue |
C | ALA113 |
C | GLN138 |
C | ARG165 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL C 282 |
Chain | Residue |
C | HIS199 |
C | PHE234 |
C | LYS52 |
C | GLN110 |
C | LYS135 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA C 283 |
Chain | Residue |
B | HOH385 |
C | ALA103 |
C | CYS106 |
C | ASN130 |
C | HOH339 |
C | HOH408 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL D 281 |
Chain | Residue |
D | LYS52 |
D | GLN110 |
D | LYS135 |
D | HIS199 |
D | PHE234 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL D 282 |
Chain | Residue |
D | ALA113 |
D | PHE114 |
D | GLN138 |
site_id | AC7 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL C 284 |
Chain | Residue |
C | ARG229 |
C | GLN274 |
C | ILE276 |
C | LEU277 |
C | HOH325 |
C | HOH327 |
C | HOH376 |
D | LEU219 |
D | LEU223 |
D | ARG263 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL D 283 |
Chain | Residue |
D | LYS82 |
D | ALA103 |
D | GLU104 |
D | ASP107 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL C 285 |
Chain | Residue |
C | ASN173 |
C | LEU174 |
C | LEU201 |
C | HOH350 |
C | HOH397 |
D | ASP177 |
D | LEU179 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL C 286 |
Chain | Residue |
C | HIS153 |
C | GLY156 |
C | ASN157 |
C | GLY158 |