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6PR9

S. aureus dihydrofolate reductase co-crystallized with 1-ethylpropyl-dihydropthalazine inhibitor and NADP(H)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004146molecular_functiondihydrofolate reductase activity
A0005829cellular_componentcytosol
A0006730biological_processone-carbon metabolic process
A0016491molecular_functionoxidoreductase activity
A0046452biological_processdihydrofolate metabolic process
A0046654biological_processtetrahydrofolate biosynthetic process
A0046655biological_processfolic acid metabolic process
A0050661molecular_functionNADP binding
Functional Information from PDB Data
site_idAC1
Number of Residues31
Detailsbinding site for residue NAP A 201
ChainResidue
AVAL6
ALYS45
ATHR46
ALEU62
ATHR63
ASER64
AHIS77
AILE79
APHE92
AGLY93
AGLY94
AALA7
AGLN95
ATHR96
AGLU100
ATHR121
AOWV202
AHOH314
AHOH321
AHOH324
AHOH333
AHOH341
AILE14
AHOH369
AHOH391
AGLY15
AASN18
AGLN19
ALEU20
AGLY43
AARG44

site_idAC2
Number of Residues15
Detailsbinding site for residue OWV A 202
ChainResidue
ALEU5
AVAL6
AALA7
AASP27
ALEU28
AVAL31
ALYS32
ASER49
AILE50
ALEU54
AARG57
APHE92
ANAP201
AHOH342
AHOH343

site_idAC3
Number of Residues5
Detailsbinding site for residue GOL A 203
ChainResidue
AARG12
APRO125
ATYR126
AGLU132
AHOH303

site_idAC4
Number of Residues10
Detailsbinding site for residue GOL A 204
ChainResidue
AILE102
AASP103
ATYR126
ATHR127
AASP130
ATRP131
AARG156
AHOH305
AHOH377
AHOH428

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
ALEU62
AGLU100
ATHR121
AGLY43
AVAL6
AILE14

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PDB entries from 2024-06-12

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