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6FCX

Structure of human 5,10-methylenetetrahydrofolate reductase (MTHFR)

Functional Information from GO Data
ChainGOidnamespacecontents
A0001666biological_processresponse to hypoxia
A0001843biological_processneural tube closure
A0003824molecular_functioncatalytic activity
A0004489molecular_functionmethylenetetrahydrofolate reductase [NAD(P)H] activity
A0005515molecular_functionprotein binding
A0005829cellular_componentcytosol
A0006555biological_processmethionine metabolic process
A0009086biological_processmethionine biosynthetic process
A0009410biological_processresponse to xenobiotic stimulus
A0016491molecular_functionoxidoreductase activity
A0033274biological_processresponse to vitamin B2
A0035999biological_processtetrahydrofolate interconversion
A0043200biological_processresponse to amino acid
A0044877molecular_functionprotein-containing complex binding
A0046500biological_processS-adenosylmethionine metabolic process
A0046653biological_processtetrahydrofolate metabolic process
A0050660molecular_functionflavin adenine dinucleotide binding
A0050661molecular_functionNADP binding
A0050667biological_processhomocysteine metabolic process
A0051593biological_processresponse to folic acid
A0070555biological_processresponse to interleukin-1
A0070828biological_processheterochromatin organization
A0071949molecular_functionFAD binding
A0072341molecular_functionmodified amino acid binding
A0106313molecular_functionmethylenetetrahydrofolate reductase (NADPH) activity
B0001666biological_processresponse to hypoxia
B0001843biological_processneural tube closure
B0003824molecular_functioncatalytic activity
B0004489molecular_functionmethylenetetrahydrofolate reductase [NAD(P)H] activity
B0005515molecular_functionprotein binding
B0005829cellular_componentcytosol
B0006555biological_processmethionine metabolic process
B0009086biological_processmethionine biosynthetic process
B0009410biological_processresponse to xenobiotic stimulus
B0016491molecular_functionoxidoreductase activity
B0033274biological_processresponse to vitamin B2
B0035999biological_processtetrahydrofolate interconversion
B0043200biological_processresponse to amino acid
B0044877molecular_functionprotein-containing complex binding
B0046500biological_processS-adenosylmethionine metabolic process
B0046653biological_processtetrahydrofolate metabolic process
B0050660molecular_functionflavin adenine dinucleotide binding
B0050661molecular_functionNADP binding
B0050667biological_processhomocysteine metabolic process
B0051593biological_processresponse to folic acid
B0070555biological_processresponse to interleukin-1
B0070828biological_processheterochromatin organization
B0071949molecular_functionFAD binding
B0072341molecular_functionmodified amino acid binding
B0106313molecular_functionmethylenetetrahydrofolate reductase (NADPH) activity
Functional Information from PDB Data
site_idAC1
Number of Residues18
Detailsbinding site for residue FAD A 701
ChainResidue
ATHR94
AALA175
AALA195
ATYR197
AHIS201
AALA204
AASP210
AHIS213
ALYS217
ATYR649
ATRP95
AHIS127
ATHR129
ALEU156
AARG157
AGLY158
AASP159
ATYR174

site_idAC2
Number of Residues16
Detailsbinding site for residue SAH A 702
ChainResidue
APRO348
AALA368
ATYR438
AASN456
ALEU460
AALA461
AGLU463
ATHR464
ATHR481
AILE482
AASN483
ASER484
AGLN485
ATHR560
ATHR573
AHOH803

site_idAC3
Number of Residues6
Detailsbinding site for residue CIT A 703
ChainResidue
AARG79
AARG82
AARG295
AARG325
AGLU326
AMET327

site_idAC4
Number of Residues4
Detailsbinding site for residue CIT B 703
ChainResidue
BARG79
BARG325
BGLU326
BMET327

site_idAC5
Number of Residues15
Detailsbinding site for Di-peptide FAD B 701 and ALA B 175
ChainResidue
BTHR94
BTRP95
BHIS127
BLEU156
BARG157
BASP159
BTYR174
BVAL176
BASP177
BALA195
BALA209
BASP210
BLEU211
BHIS213
BTYR321

site_idAC6
Number of Residues15
Detailsbinding site for Di-peptide FAD B 701 and ASP B 210
ChainResidue
BTHR94
BTRP95
BHIS127
BLEU156
BARG157
BASP159
BALA175
BALA195
BSER206
BALA209
BLEU211
BLYS212
BHIS213
BLEU214
BTYR321

site_idAC7
Number of Residues20
Detailsbinding site for Di-peptide SAH B 702 and GLN B 485
ChainResidue
BPRO348
BALA368
BASN456
BLEU460
BALA461
BGLU463
BTHR464
BTHR481
BILE482
BASN483
BSER484
BPRO486
BGLN509
BLYS510
BALA511
BTYR512
BVAL559
BTHR560
BTHR573
BHOH815

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues20
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues37
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"29891918","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"29891918","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"29891918","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues3
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"29891918","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

243083

PDB entries from 2025-10-15

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