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3FRA

Staphylococcus aureus F98Y DHFR complexed with iclaprim

Functional Information from GO Data
ChainGOidnamespacecontents
X0004146molecular_functiondihydrofolate reductase activity
X0005829cellular_componentcytosol
X0006730biological_processone-carbon metabolic process
X0016491molecular_functionoxidoreductase activity
X0046452biological_processdihydrofolate metabolic process
X0046654biological_processtetrahydrofolate biosynthetic process
X0046655biological_processfolic acid metabolic process
X0050661molecular_functionNADP binding
Functional Information from PDB Data
site_idAC1
Number of Residues28
DetailsBINDING SITE FOR RESIDUE NAP X 301
ChainResidue
XVAL6
XLYS45
XTHR46
XLEU62
XTHR63
XSER64
XPHE92
XGLY93
XGLY94
XGLN95
XTHR96
XALA7
XTYR98
XGLU100
XTHR121
XHOH177
XHOH178
XHOH179
XHOH180
XHOH258
XI2H300
XILE14
XGLY15
XASN18
XGLN19
XLEU20
XGLY43
XARG44

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE I2H X 300
ChainResidue
XLEU5
XVAL6
XALA7
XASP27
XLEU28
XVAL31
XSER49
XPHE92
XTYR98
XHOH160
XHOH196
XHOH216
XNAP301

Functional Information from PROSITE/UniProt
site_idPS00075
Number of Residues23
DetailsDHFR_1 Dihydrofolate reductase (DHFR) domain signature. VIGfenqLPWhlpn.DlkhVkklS
ChainResidueDetails
XVAL13-SER35

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING: BINDING => ECO:0000305|PubMed:19280600
ChainResidueDetails
XLEU5
XASP27
XSER49
XARG57
XPHE92

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:19280600
ChainResidueDetails
XVAL6
XILE14
XGLY43
XLEU62
XGLU100
XTHR121

222036

PDB entries from 2024-07-03

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