6DE8
Crystal Structure of Bifunctional Enzyme FolD-Methylenetetrahydrofolate Dehydrogenase/Cyclohydrolase 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 | 1 |
| Details | binding site for residue IOD A 301 |
| Chain | Residue |
| A | ILE189 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | binding site for residue IOD A 302 |
| Chain | Residue |
| A | PRO258 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | binding site for residue IOD A 303 |
| Chain | Residue |
| A | ASN167 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue IOD A 304 |
| Chain | Residue |
| A | LEU98 |
| A | LYS104 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue IOD A 305 |
| Chain | Residue |
| A | LYS278 |
| B | ASN70 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | binding site for residue IOD A 307 |
| Chain | Residue |
| A | GOL310 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | binding site for residue IOD A 309 |
| Chain | Residue |
| A | LYS49 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 310 |
| Chain | Residue |
| A | SER10 |
| A | LYS14 |
| A | PRO263 |
| A | ILE266 |
| A | IOD307 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | binding site for residue IOD B 302 |
| Chain | Residue |
| B | LYS49 |
| B | HIS66 |
| site_id | AD1 |
| Number of Residues | 1 |
| Details | binding site for residue IOD B 303 |
| Chain | Residue |
| B | PRO263 |
| site_id | AD2 |
| Number of Residues | 1 |
| Details | binding site for residue IOD B 307 |
| Chain | Residue |
| B | K311 |
| site_id | AD3 |
| Number of Residues | 1 |
| Details | binding site for residue IOD B 308 |
| Chain | Residue |
| B | LEU98 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 309 |
| Chain | Residue |
| B | SER114 |
| B | PHE136 |
| B | LYS275 |
| B | SER276 |
| B | ASN279 |
| B | ARG280 |
| site_id | AD5 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 310 |
| Chain | Residue |
| B | ASN68 |
| B | ILE71 |
| site_id | AD6 |
| Number of Residues | 1 |
| Details | binding site for residue K B 311 |
| Chain | Residue |
| B | IOD307 |
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 |
