3L07
Methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase, putative bifunctional protein folD from Francisella tularensis.
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 | 5 |
Details | BINDING SITE FOR RESIDUE PO4 A 501 |
Chain | Residue |
A | GLY165 |
A | ALA166 |
A | HIS189 |
A | ARG190 |
A | HOH353 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE IMD B 502 |
Chain | Residue |
B | HOH438 |
B | ILE231 |
B | PRO258 |
B | GLY259 |
B | HOH327 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE IMD A 503 |
Chain | Residue |
A | PRO258 |
A | GLY259 |
A | PRO263 |
A | HOH317 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO B 504 |
Chain | Residue |
B | LYS143 |
B | THR147 |
B | ARG150 |
B | GLU268 |
B | TYR271 |
B | HOH355 |
B | HOH389 |
site_id | AC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE EDO B 505 |
Chain | Residue |
B | ARG16 |
B | GLN20 |
B | ALA101 |
B | HIS102 |
B | ILE103 |
B | ASN104 |
B | TYR271 |
B | HOH332 |
B | HOH344 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 506 |
Chain | Residue |
A | LYS143 |
A | GLU268 |
A | TYR271 |
A | HOH437 |
A | HOH461 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 507 |
Chain | Residue |
A | LEU94 |
A | VAL95 |
A | ASP119 |
A | PHE121 |
A | HOH296 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ACT B 508 |
Chain | Residue |
B | GLY165 |
B | ALA166 |
B | HIS189 |
B | ARG190 |
B | HOH406 |
B | HOH475 |
Functional Information from PROSITE/UniProt
site_id | PS00766 |
Number of Residues | 26 |
Details | THF_DHG_CYH_1 Tetrahydrofolate dehydrogenase/cyclohydrolase signature 1. EsELLelIdqLNnDssvhaILVQLPL |
Chain | Residue | Details |
A | GLU74-LEU99 |
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 | 4 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01576 |
Chain | Residue | Details |
A | GLY165 | |
A | ILE231 | |
B | GLY165 | |
B | ILE231 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1a4i |
Chain | Residue | Details |
A | LYS52 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1a4i |
Chain | Residue | Details |
B | LYS52 |