6FCX
Structure of human 5,10-methylenetetrahydrofolate reductase (MTHFR)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0001666 | biological_process | response to hypoxia |
A | 0001843 | biological_process | neural tube closure |
A | 0003824 | molecular_function | catalytic activity |
A | 0004489 | molecular_function | methylenetetrahydrofolate reductase [NAD(P)H] activity |
A | 0005515 | molecular_function | protein binding |
A | 0005829 | cellular_component | cytosol |
A | 0006555 | biological_process | methionine metabolic process |
A | 0009086 | biological_process | methionine biosynthetic process |
A | 0009410 | biological_process | response to xenobiotic stimulus |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0033274 | biological_process | response to vitamin B2 |
A | 0035999 | biological_process | tetrahydrofolate interconversion |
A | 0043200 | biological_process | response to amino acid |
A | 0044877 | molecular_function | protein-containing complex binding |
A | 0046500 | biological_process | S-adenosylmethionine metabolic process |
A | 0046653 | biological_process | tetrahydrofolate metabolic process |
A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
A | 0050661 | molecular_function | NADP binding |
A | 0050667 | biological_process | homocysteine metabolic process |
A | 0051593 | biological_process | response to folic acid |
A | 0070555 | biological_process | response to interleukin-1 |
A | 0070828 | biological_process | heterochromatin organization |
A | 0071949 | molecular_function | FAD binding |
A | 0072341 | molecular_function | modified amino acid binding |
A | 0106313 | molecular_function | methylenetetrahydrofolate reductase (NADPH) activity |
B | 0001666 | biological_process | response to hypoxia |
B | 0001843 | biological_process | neural tube closure |
B | 0003824 | molecular_function | catalytic activity |
B | 0004489 | molecular_function | methylenetetrahydrofolate reductase [NAD(P)H] activity |
B | 0005515 | molecular_function | protein binding |
B | 0005829 | cellular_component | cytosol |
B | 0006555 | biological_process | methionine metabolic process |
B | 0009086 | biological_process | methionine biosynthetic process |
B | 0009410 | biological_process | response to xenobiotic stimulus |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0033274 | biological_process | response to vitamin B2 |
B | 0035999 | biological_process | tetrahydrofolate interconversion |
B | 0043200 | biological_process | response to amino acid |
B | 0044877 | molecular_function | protein-containing complex binding |
B | 0046500 | biological_process | S-adenosylmethionine metabolic process |
B | 0046653 | biological_process | tetrahydrofolate metabolic process |
B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
B | 0050661 | molecular_function | NADP binding |
B | 0050667 | biological_process | homocysteine metabolic process |
B | 0051593 | biological_process | response to folic acid |
B | 0070555 | biological_process | response to interleukin-1 |
B | 0070828 | biological_process | heterochromatin organization |
B | 0071949 | molecular_function | FAD binding |
B | 0072341 | molecular_function | modified amino acid binding |
B | 0106313 | molecular_function | methylenetetrahydrofolate reductase (NADPH) activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 18 |
Details | binding site for residue FAD A 701 |
Chain | Residue |
A | THR94 |
A | ALA175 |
A | ALA195 |
A | TYR197 |
A | HIS201 |
A | ALA204 |
A | ASP210 |
A | HIS213 |
A | LYS217 |
A | TYR649 |
A | TRP95 |
A | HIS127 |
A | THR129 |
A | LEU156 |
A | ARG157 |
A | GLY158 |
A | ASP159 |
A | TYR174 |
site_id | AC2 |
Number of Residues | 16 |
Details | binding site for residue SAH A 702 |
Chain | Residue |
A | PRO348 |
A | ALA368 |
A | TYR438 |
A | ASN456 |
A | LEU460 |
A | ALA461 |
A | GLU463 |
A | THR464 |
A | THR481 |
A | ILE482 |
A | ASN483 |
A | SER484 |
A | GLN485 |
A | THR560 |
A | THR573 |
A | HOH803 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue CIT A 703 |
Chain | Residue |
A | ARG79 |
A | ARG82 |
A | ARG295 |
A | ARG325 |
A | GLU326 |
A | MET327 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue CIT B 703 |
Chain | Residue |
B | ARG79 |
B | ARG325 |
B | GLU326 |
B | MET327 |
site_id | AC5 |
Number of Residues | 15 |
Details | binding site for Di-peptide FAD B 701 and ALA B 175 |
Chain | Residue |
B | THR94 |
B | TRP95 |
B | HIS127 |
B | LEU156 |
B | ARG157 |
B | ASP159 |
B | TYR174 |
B | VAL176 |
B | ASP177 |
B | ALA195 |
B | ALA209 |
B | ASP210 |
B | LEU211 |
B | HIS213 |
B | TYR321 |
site_id | AC6 |
Number of Residues | 15 |
Details | binding site for Di-peptide FAD B 701 and ASP B 210 |
Chain | Residue |
B | THR94 |
B | TRP95 |
B | HIS127 |
B | LEU156 |
B | ARG157 |
B | ASP159 |
B | ALA175 |
B | ALA195 |
B | SER206 |
B | ALA209 |
B | LEU211 |
B | LYS212 |
B | HIS213 |
B | LEU214 |
B | TYR321 |
site_id | AC7 |
Number of Residues | 20 |
Details | binding site for Di-peptide SAH B 702 and GLN B 485 |
Chain | Residue |
B | PRO348 |
B | ALA368 |
B | ASN456 |
B | LEU460 |
B | ALA461 |
B | GLU463 |
B | THR464 |
B | THR481 |
B | ILE482 |
B | ASN483 |
B | SER484 |
B | PRO486 |
B | GLN509 |
B | LYS510 |
B | ALA511 |
B | TYR512 |
B | VAL559 |
B | THR560 |
B | THR573 |
B | HOH815 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 20 |
Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 37 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"29891918","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"29891918","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"29891918","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 3 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"29891918","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |