4B4U
Crystal structure of Acinetobacter baumannii N5, N10- methylenetetrahydrofolate dehydrogenase-cyclohydrolase (FolD) complexed with NADP cofactor
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000105 | biological_process | histidine biosynthetic process |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004477 | molecular_function | methenyltetrahydrofolate cyclohydrolase activity |
| A | 0004488 | molecular_function | methylenetetrahydrofolate dehydrogenase (NADP+) activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006164 | biological_process | purine nucleotide biosynthetic process |
| A | 0006730 | biological_process | one-carbon metabolic process |
| A | 0009086 | biological_process | methionine biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0035999 | biological_process | tetrahydrofolate interconversion |
| B | 0000105 | biological_process | histidine biosynthetic process |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004477 | molecular_function | methenyltetrahydrofolate cyclohydrolase activity |
| B | 0004488 | molecular_function | methylenetetrahydrofolate dehydrogenase (NADP+) activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006164 | biological_process | purine nucleotide biosynthetic process |
| B | 0006730 | biological_process | one-carbon metabolic process |
| B | 0009086 | biological_process | methionine biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0035999 | biological_process | tetrahydrofolate interconversion |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE NAP A 1001 |
| Chain | Residue |
| A | GLY165 |
| A | HOH2290 |
| A | HOH2327 |
| A | HOH2382 |
| A | HOH2383 |
| A | HOH2384 |
| A | HOH2385 |
| A | HOH2386 |
| A | ARG166 |
| A | SER167 |
| A | HIS189 |
| A | SER190 |
| A | ALA208 |
| A | VAL209 |
| A | LYS211 |
| A | LEU214 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE NAP B 1001 |
| Chain | Residue |
| B | GLY165 |
| B | ARG166 |
| B | SER167 |
| B | HIS189 |
| B | SER190 |
| B | ALA208 |
| B | VAL209 |
| B | LYS211 |
| B | LEU214 |
| B | HOH2255 |
| B | HOH2287 |
| B | HOH2344 |
| B | HOH2345 |
| B | HOH2346 |
| B | HOH2347 |
| B | HOH2348 |
| B | HOH2350 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 1283 |
| Chain | Residue |
| A | ARG51 |
| A | ARG58 |
| A | HOH2108 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 1284 |
| Chain | Residue |
| A | ARG59 |
| A | HOH2142 |
| B | ARG59 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 1285 |
| Chain | Residue |
| A | GLN180 |
| B | ARG166 |
| B | LYS172 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 1283 |
| Chain | Residue |
| A | ARG166 |
| A | LYS172 |
| B | LEU179 |
| B | GLN180 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL B 1284 |
| Chain | Residue |
| B | GLN71 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO A 1286 |
| Chain | Residue |
| A | ARG8 |
| A | PHE231 |
| A | PRO258 |
| A | GLY259 |
| A | GLY262 |
| A | PRO263 |
| A | HOH2365 |
| A | HOH2387 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 1285 |
| Chain | Residue |
| B | GLN222 |
| B | GLY223 |
| B | ALA251 |
| B | SER252 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 1286 |
| Chain | Residue |
| B | PHE231 |
| B | PRO258 |
| B | GLY259 |
| B | PRO263 |
| B | HOH2324 |
| B | HOH2330 |
| B | HOH2351 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 1287 |
| Chain | Residue |
| A | MET132 |
| B | ARG107 |
| B | ALA168 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 1287 |
| Chain | Residue |
| A | GLU106 |
| A | ARG107 |
| A | ALA168 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PEG A 1288 |
| Chain | Residue |
| A | ALA136 |
| A | TYR137 |
| A | HOH2238 |
| A | HOH2239 |
Functional Information from PROSITE/UniProt
| site_id | PS00136 |
| Number of Residues | 12 |
| Details | SUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. AVVVDAGFhprD |
| Chain | Residue | Details |
| A | ALA224-ASP235 |
| site_id | PS00767 |
| Number of Residues | 9 |
| Details | THF_DHG_CYH_2 Tetrahydrofolate dehydrogenase/cyclohydrolase signature 2. PGGVGPMTI |
| Chain | Residue | Details |
| A | PRO258-ILE266 |
