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6PBO

Staphylococcus aureus Dihydrofolate reductase in complex with NADPH and UCP1232

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 Residues15
Detailsbinding site for residue O71 X 201
ChainResidue
XLEU5
XARG57
XPHE92
XTHR111
XXNP202
XNAP203
XHOH326
XVAL6
XALA7
XLEU20
XASP27
XLEU28
XVAL31
XLYS32
XILE50

site_idAC2
Number of Residues24
Detailsbinding site for residue XNP X 202
ChainResidue
XILE14
XASN18
XGLN19
XLEU20
XGLY43
XARG44
XLYS45
XTHR46
XLEU62
XTHR63
XSER64
XGLY94
XGLN95
XTHR96
XGLU100
XTHR121
XO71201
XNAP203
XHOH301
XHOH304
XHOH309
XHOH321
XHOH338
XHOH339

site_idAC3
Number of Residues29
Detailsbinding site for residue NAP X 203
ChainResidue
XVAL6
XALA7
XILE14
XGLY15
XGLN19
XGLY43
XARG44
XLYS45
XTHR46
XLEU62
XTHR63
XSER64
XHIS77
XILE79
XPHE92
XGLY93
XGLY94
XGLN95
XTHR96
XLEU97
XGLU100
XTHR121
XO71201
XXNP202
XHOH301
XHOH309
XHOH321
XHOH338
XHOH339

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 2024-07-17

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