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6MT8

E. coli DHFR complex modeled with two ligand states

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 Residues5
Detailsbinding site for residue CL A 201
ChainResidue
AGLY43
AHIS45
ATHR46
AGLY96
AHOH432

site_idAC2
Number of Residues5
Detailsbinding site for residue CL A 202
ChainResidue
AHOH480
ALYS32
AASP144
AALA145
AHOH417

site_idAC3
Number of Residues3
Detailsbinding site for residue CL A 203
ChainResidue
ATRP30
AARG33
AHOH368

site_idAC4
Number of Residues6
Detailsbinding site for residue MG A 204
ChainResidue
AGLU101
AGLU139
AHOH336
AHOH352
AHOH388
AHOH420

site_idAC5
Number of Residues5
Detailsbinding site for residue MG A 205
ChainResidue
AGLU101
ASER138
AHOH370
AHOH445
AHOH457

site_idAC6
Number of Residues6
Detailsbinding site for residue MG A 206
ChainResidue
AHIS160
AHOH326
AHOH380
AHOH415
AHOH443
AHOH486

site_idAC7
Number of Residues6
Detailsbinding site for residue MG A 207
ChainResidue
AASP70
AHOH313
AHOH341
AHOH385
AHOH392
AHOH465

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

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PDB entries from 2024-07-17

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