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6PR8

S. aureus dihydrofoate reductase co-crystallized with 3,5-dimethylphenyl-dihydropthalazine inhibitor and NADP(H)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004146molecular_functiondihydrofolate reductase activity
A0006730biological_processone-carbon metabolic process
A0016491molecular_functionoxidoreductase activity
A0046654biological_processtetrahydrofolate biosynthetic process
A0050661molecular_functionNADP binding
Functional Information from PDB Data
site_idAC1
Number of Residues17
Detailsbinding site for residue OWJ A 301
ChainResidue
ALEU5
ALEU54
APRO55
AARG57
APHE92
ATHR111
ANAP302
AHOH413
AHOH453
AVAL6
AALA7
AASP27
ALEU28
ALYS29
AVAL31
ALYS32
ASER49

site_idAC2
Number of Residues32
Detailsbinding site for residue NAP A 302
ChainResidue
AVAL6
AALA7
AILE14
AGLY15
AASN18
AGLN19
ALEU20
AGLY43
AARG44
ALYS45
ATHR46
ALEU62
ATHR63
ASER64
AHIS77
AILE79
APHE92
AGLY93
AGLY94
AGLN95
ATHR96
ALEU97
AGLU100
ATHR121
AOWJ301
AHOH423
AHOH428
AHOH429
AHOH448
AHOH457
AHOH461
AHOH462

site_idAC3
Number of Residues6
Detailsbinding site for residue GOL A 303
ChainResidue
AARG12
APRO125
ATYR126
AGLU132
AHOH402
AHOH436

site_idAC4
Number of Residues10
Detailsbinding site for residue GOL A 304
ChainResidue
AILE102
AASP103
ATYR126
ATHR127
AASP130
ATRP131
AARG156
AHOH406
AHOH478
AHOH531

Functional Information from PROSITE/UniProt
site_idPS00075
Number of Residues23
DetailsDHFR_1 Dihydrofolate reductase (DHFR) domain signature. VIGfenqLPWhlpn.DlkhVkklS
ChainResidueDetails
AVAL13-SER35

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING: BINDING => ECO:0000305|PubMed:19280600
ChainResidueDetails
ALEU5
AASP27
ASER49
AARG57
APHE92

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:19280600
ChainResidueDetails
AVAL6
AILE14
AGLY43
ALEU62
AGLU100
ATHR121

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PDB entries from 2024-07-24

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