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5UIH

structure of DHFR with bound phenformin and NADP

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 Residues9
Detailsbinding site for residue 8CV A 201
ChainResidue
AILE5
AMET16
AASP27
ALEU28
APHE31
AILE94
ATYR100
AHOH358
AHOH433

site_idAC2
Number of Residues3
Detailsbinding site for residue NA A 202
ChainResidue
AHOH361
AHOH366
AHOH397

site_idAC3
Number of Residues26
Detailsbinding site for residue NAP A 203
ChainResidue
AGLY43
AARG44
AHIS45
ATHR46
ALEU62
ASER63
ASER64
ALYS76
AGLY96
AGLY97
AARG98
AVAL99
AGLN102
ATHR123
APHE137
AGLU139
APHE140
AHOH324
AHOH341
AHOH350
AHOH362
AHOH375
AHOH406
AHOH410
AHOH424
AHOH445

site_idAC4
Number of Residues7
Detailsbinding site for residue BME A 204
ChainResidue
AHIS114
ASER138
APHE140
ACYS152
APHE153
AGLU154
AHOH322

site_idAC5
Number of Residues6
Detailsbinding site for residue EDO A 205
ChainResidue
ALYS58
AASN59
AARG71
ATHR73
AHOH396
AHOH411

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

223790

PDB entries from 2024-08-14

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