Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3FRE

S. aureus DHFR complexed with NADPH and TMP

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 Residues27
DetailsBINDING SITE FOR RESIDUE NDP X 301
ChainResidue
XVAL6
XLYS45
XTHR46
XLEU62
XTHR63
XSER64
XILE79
XPHE92
XGLY93
XGLY94
XGLN95
XALA7
XTHR96
XGLU100
XTHR121
XHOH164
XHOH167
XHOH181
XHOH182
XTOP300
XILE14
XGLY15
XASN18
XGLN19
XLEU20
XGLY43
XARG44

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE TOP X 300
ChainResidue
XLEU5
XVAL6
XALA7
XASP27
XLEU28
XVAL31
XSER49
XPHE92
XHOH163
XHOH255
XNDP301

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
XLEU62
XGLU100
XTHR121
XVAL6
XILE14
XGLY43

219869

PDB entries from 2024-05-15

PDB statisticsPDBj update infoContact PDBjnumon