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7DFR

CRYSTAL STRUCTURES OF ESCHERICHIA COLI DIHYDROFOLATE REDUCTASE. THE NADP+ HOLOENZYME AND THE FOLATE(DOT)NADP+ TERNARY COMPLEX. SUBSTRATE BINDING AND A MODEL FOR THE TRANSITION STATE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004146molecular_functiondihydrofolate reductase activity
A0005515molecular_functionprotein binding
A0005542molecular_functionfolic acid binding
A0005829cellular_componentcytosol
A0006730biological_processone-carbon metabolic process
A0009257biological_process10-formyltetrahydrofolate biosynthetic 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
A0046656biological_processfolic acid biosynthetic process
A0046677biological_processresponse to antibiotic
A0050661molecular_functionNADP binding
A0051870molecular_functionmethotrexate binding
A0051871molecular_functiondihydrofolic acid binding
A0070401molecular_functionNADP+ binding
A0070402molecular_functionNADPH binding
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE FOL A 161
ChainResidue
AILE5
AARG57
AILE94
ATHR113
ANAP164
AHOH206
AHOH301
AALA7
AMET20
AASP27
ALEU28
APHE31
ALYS32
ATHR46
AILE50

site_idAC2
Number of Residues27
DetailsBINDING SITE FOR RESIDUE NAP A 164
ChainResidue
AALA6
AALA7
AILE14
AMET16
AASN18
AALA19
AMET20
ATRP22
AGLY43
AARG44
AHIS45
ATHR46
ASER49
ALEU62
ASER63
ASER64
ALYS76
AILE94
AGLY96
AGLY97
AARG98
AVAL99
ATYR100
AGLN102
AFOL161
AHOH225
AHOH237

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 Residues5
DetailsBINDING: BINDING => ECO:0000305|PubMed:9012674
ChainResidueDetails
AILE5
AASP27
AARG52
AARG57
ATHR113

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:19374017
ChainResidueDetails
AALA7
AVAL13
AHIS45
ASER63
ALYS76
AGLY95

Catalytic Information from CSA
site_idCSA1
Number of Residues7
DetailsAnnotated By Reference To The Literature 1ra2
ChainResidueDetails
ALEU54
ALEU28
APHE31
AASP27
AILE5
AMET20
AILE94

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PDB entries from 2024-10-30

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