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6ND2

Staphylococcus aureus Dihydrofolate Reductase complexed with NADPH and 6-ETHYL-5-[(3R)-3-[2-METHOXY-5-(PYRIDIN-4-YL)PHENYL]BUT-1-YN-1-YL]PYRIMIDINE-2,4-DIAMINE (UCP1063)

Functional Information from GO Data
ChainGOidnamespacecontents
X0004146molecular_functiondihydrofolate reductase activity
X0006730biological_processone-carbon metabolic process
X0016491molecular_functionoxidoreductase activity
X0046654biological_processtetrahydrofolate biosynthetic process
X0050661molecular_functionNADP binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue GOL X 201
ChainResidue
XARG12
XPRO125
XTYR126
XGLU132
XHOH310

site_idAC2
Number of Residues15
Detailsbinding site for residue G8J X 202
ChainResidue
XLEU20
XASP27
XLEU28
XVAL31
XTHR46
XSER49
XILE50
XLEU54
XPHE92
XXNP203
XHOH324
XLEU5
XVAL6
XALA7
XASN18

site_idAC3
Number of Residues26
Detailsbinding site for residue XNP X 203
ChainResidue
XILE14
XGLY15
XASN18
XGLY43
XARG44
XLYS45
XTHR46
XSER49
XLEU62
XTHR63
XSER64
XSER67
XHIS77
XILE79
XGLY94
XGLN95
XTHR96
XLEU97
XGLU100
XG8J202
XHOH301
XHOH302
XHOH314
XHOH316
XHOH321
XHOH325

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

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PDB entries from 2024-07-24

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