6DEB
Crystal Structure of Bifunctional Enzyme FolD-Methylenetetrahydrofolate Dehydrogenase/Cyclohydrolase in the Complex with Methotrexate 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 | 6 |
| Details | binding site for residue GUN A 301 |
| Chain | Residue |
| A | VAL94 |
| A | LEU96 |
| A | ASP118 |
| A | THR140 |
| A | ILE168 |
| A | HOH491 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue K A 302 |
| Chain | Residue |
| B | ASP100 |
| B | ILE102 |
| B | HOH487 |
| B | HOH573 |
| A | MET1 |
| A | THR2 |
| A | HOH603 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 303 |
| Chain | Residue |
| A | GLU133 |
| A | LEU142 |
| A | MET145 |
| A | HOH509 |
| A | HOH575 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 304 |
| Chain | Residue |
| A | PRO258 |
| A | GLY259 |
| A | HOH580 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 305 |
| Chain | Residue |
| A | HIS188 |
| A | ILE189 |
| A | HOH423 |
| A | HOH456 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 306 |
| Chain | Residue |
| A | ALA165 |
| A | ARG171 |
| A | HIS188 |
| A | HOH443 |
| B | LEU178 |
| B | ASN179 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue TRS B 301 |
| Chain | Residue |
| A | ASN129 |
| A | ARG171 |
| A | ALA174 |
| A | THR175 |
| B | ASN129 |
| B | ARG171 |
| B | THR175 |
| site_id | AC8 |
| Number of Residues | 12 |
| Details | binding site for residue MTX B 302 |
| Chain | Residue |
| B | LEU93 |
| B | VAL94 |
| B | GLN95 |
| B | LEU96 |
| B | LYS104 |
| B | ASP118 |
| B | THR140 |
| B | ILE168 |
| B | VAL169 |
| B | MTX303 |
| B | HOH426 |
| B | HOH567 |
| site_id | AC9 |
| Number of Residues | 13 |
| Details | binding site for residue MTX B 303 |
| Chain | Residue |
| A | SER26 |
| A | LYS27 |
| B | TYR47 |
| B | LYS51 |
| B | GLN95 |
| B | ALA208 |
| B | GLY209 |
| B | VAL228 |
| B | MTX302 |
| B | HOH419 |
| B | HOH420 |
| B | HOH537 |
| B | HOH557 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue CL B 304 |
| Chain | Residue |
| B | PRO258 |
| B | GLY259 |
| B | HOH571 |
| B | HOH630 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 305 |
| Chain | Residue |
| B | GLU133 |
| B | MET145 |
| B | HOH498 |
| B | HOH503 |
| B | HOH522 |
| site_id | AD3 |
| Number of Residues | 8 |
| Details | binding site for residue DTT B 306 |
| Chain | Residue |
| A | LEU178 |
| A | ASN179 |
| A | GLY181 |
| B | ALA165 |
| B | ARG171 |
| B | HIS188 |
| B | LYS190 |
| B | HOH432 |
| site_id | AD4 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 307 |
| Chain | Residue |
| B | HIS188 |
| B | ILE189 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 308 |
| Chain | Residue |
| B | ASP193 |
| B | LEU194 |
| B | SER195 |
| B | HOH482 |
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 |
