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1DYH

ISOMORPHOUS CRYSTAL STRUCTURES OF ESCHERICHIA COLI DIHYDROFOLATE REDUCTASE COMPLEXED WITH FOLATE, 5-DEAZAFOLATE AND 5,10-DIDEAZATETRAHYDROFOLATE: MECHANISTIC IMPLICATIONS

Functional Information from GO Data
ChainGOidnamespacecontents
A0004146molecular_functiondihydrofolate reductase activity
A0005515molecular_functionprotein binding
A0005542molecular_functionfolic acid binding
A0005829cellular_componentcytosol
A0006545biological_processglycine biosynthetic process
A0006730biological_processone-carbon metabolic process
A0009410biological_processresponse to xenobiotic stimulus
A0016491molecular_functionoxidoreductase activity
A0031427biological_processresponse to methotrexate
A0046452biological_processdihydrofolate metabolic process
A0046654biological_processtetrahydrofolate biosynthetic process
A0046655biological_processfolic acid metabolic process
A0046677biological_processresponse to antibiotic
A0050661molecular_functionNADP binding
A0051870molecular_functionmethotrexate binding
A0051871molecular_functiondihydrofolic acid binding
A0070401molecular_functionNADP+ binding
A0070402molecular_functionNADPH binding
B0004146molecular_functiondihydrofolate reductase activity
B0005515molecular_functionprotein binding
B0005542molecular_functionfolic acid binding
B0005829cellular_componentcytosol
B0006545biological_processglycine biosynthetic process
B0006730biological_processone-carbon metabolic process
B0009410biological_processresponse to xenobiotic stimulus
B0016491molecular_functionoxidoreductase activity
B0031427biological_processresponse to methotrexate
B0046452biological_processdihydrofolate metabolic process
B0046654biological_processtetrahydrofolate biosynthetic process
B0046655biological_processfolic acid metabolic process
B0046677biological_processresponse to antibiotic
B0050661molecular_functionNADP binding
B0051870molecular_functionmethotrexate binding
B0051871molecular_functiondihydrofolic acid binding
B0070401molecular_functionNADP+ binding
B0070402molecular_functionNADPH binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 401
ChainResidue
AGLY43
AHIS45
ATHR46
AGLY96
AHOH468

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 405
ChainResidue
BGLY43
BHIS45
BTHR46
BGLY96

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 420
ChainResidue
AHOH488
BSER135
BHOH461
BHOH462
BHOH464
BHOH476

site_idAC4
Number of Residues17
DetailsBINDING SITE FOR RESIDUE DZF A 161
ChainResidue
AILE5
AALA6
AALA7
AASP27
ALEU28
APHE31
ATHR46
AILE50
AARG52
AARG57
AILE94
ATHR113
AHOH403
AHOH405
AHOH501
AHOH560
AHOH566

site_idAC5
Number of Residues18
DetailsBINDING SITE FOR RESIDUE DZF B 161
ChainResidue
BILE5
BALA6
BALA7
BASP27
BLEU28
BPHE31
BLYS32
BILE50
BARG52
BARG57
BILE94
BTYR100
BTHR113
BHOH426
BHOH459
BHOH518
BHOH570
BHOH612

Functional Information from PROSITE/UniProt
site_idPS00075
Number of Residues23
DetailsDHFR_1 Dihydrofolate reductase (DHFR) domain signature. VIGmenaMPWnlpa.DlawFkrnT
ChainResidueDetails
AVAL13-THR35

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000305|PubMed:9012674
ChainResidueDetails
AILE5
BTHR113
AASP27
AARG52
AARG57
ATHR113
BILE5
BASP27
BARG52
BARG57

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:19374017
ChainResidueDetails
AALA7
BSER63
BLYS76
BGLY95
AVAL13
AHIS45
ASER63
ALYS76
AGLY95
BALA7
BVAL13
BHIS45

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PDB entries from 2024-03-27

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