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6XG4

X-ray structure of Escherichia coli dihydrofolate reductase L28R mutant in complex with trimethoprim

Functional Information from GO Data
ChainGOidnamespacecontents
A0004146molecular_functiondihydrofolate reductase activity
A0005515molecular_functionprotein binding
A0005542molecular_functionfolic acid binding
A0005829cellular_componentcytosol
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
Functional Information from PDB Data
site_idAC1
Number of Residues29
Detailsbinding site for residue NDP A 301
ChainResidue
AALA6
AHIS45
ATHR46
ALEU62
ASER63
ASER64
ALYS76
AVAL78
AILE94
AGLY96
AGLY97
AALA7
AARG98
AVAL99
ATYR100
AGLN102
ATOP303
AHOH407
AHOH427
AHOH432
AHOH433
AHOH446
AILE14
AGLY15
AASN18
AALA19
AMET20
AGLY43
AARG44

site_idAC2
Number of Residues7
Detailsbinding site for residue GOL A 302
ChainResidue
AVAL10
AASP116
ASER148
AHIS149
ASER150
AHOH408
AHOH434

site_idAC3
Number of Residues14
Detailsbinding site for residue TOP A 303
ChainResidue
AILE5
AALA6
AMET20
AASP27
APHE31
ASER49
AILE50
AILE94
ATYR100
ANDP301
AHOH409
AHOH440
AHOH470
AHOH520

site_idAC4
Number of Residues2
Detailsbinding site for residue CL A 304
ChainResidue
AARG98
AGLN102

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING: BINDING => ECO:0000305|PubMed:9012674
ChainResidueDetails
ATHR113
AILE5
AASP27
AARG52
AARG57

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

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PDB entries from 2024-06-12

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