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 | 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 | 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 | 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 |