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 | 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 | 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 | 6 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01576, ECO:0000269|Ref.2 |
Chain | Residue | Details |
A | GLY164 | |
A | ILE189 | |
A | ILE230 | |
B | GLY164 | |
B | ILE189 | |
B | ILE230 |