3P2O
Crystal Structure of FolD Bifunctional Protein from Campylobacter jejuni
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000105 | biological_process | L-histidine biosynthetic process |
| 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 | 0008652 | biological_process | amino acid biosynthetic 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 | L-histidine biosynthetic process |
| 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 | 0008652 | biological_process | amino acid biosynthetic 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 | 18 |
| Details | BINDING SITE FOR RESIDUE NAD A 291 |
| Chain | Residue |
| A | THR140 |
| A | LEU213 |
| A | VAL228 |
| A | GLY229 |
| A | ILE230 |
| A | GLY262 |
| A | HOH290 |
| A | HOH305 |
| A | HOH314 |
| A | HOH326 |
| A | GLY164 |
| A | ALA165 |
| A | SER166 |
| A | HIS188 |
| A | ILE189 |
| A | ALA207 |
| A | ALA208 |
| A | GLY209 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 292 |
| Chain | Residue |
| A | ASN129 |
| A | ARG171 |
| A | THR175 |
| B | ASN129 |
| B | ARG171 |
| B | THR175 |
| site_id | AC3 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE NAD B 291 |
| Chain | Residue |
| B | TYR47 |
| B | THR140 |
| B | GLY164 |
| B | ALA165 |
| B | SER166 |
| B | VAL169 |
| B | HIS188 |
| B | ILE189 |
| B | ALA207 |
| B | ALA208 |
| B | GLY209 |
| B | CYS210 |
| B | VAL228 |
| B | GLY229 |
| B | ILE230 |
| B | GLY262 |
| B | THR265 |
| B | HOH298 |
| B | HOH305 |
Functional Information from PROSITE/UniProt
| site_id | PS00766 |
| Number of Residues | 26 |
| Details | THF_DHG_CYH_1 Tetrahydrofolate dehydrogenase/cyclohydrolase signature 1. QnELLalIntLNhDdsvhgILVQLPL |
| Chain | Residue | Details |
| A | GLN73-LEU98 |
| site_id | PS00767 |
| Number of Residues | 9 |
| Details | THF_DHG_CYH_2 Tetrahydrofolate dehydrogenase/cyclohydrolase signature 2. PGGVGPMTI |
| Chain | Residue | Details |
| A | PRO258-ILE266 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01576","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"OCT-2010","submissionDatabase":"PDB data bank","title":"Crystal structure of FolD bifunctional protein.","authoringGroup":["Center for structural genomics of infectious diseases (CSGID)"]}}]} |
| Chain | Residue | Details |
