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3M08

Wild Type Dihydrofolate Reductase from Staphylococcus aureus with inhibitor RAB1

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 Residues20
DetailsBINDING SITE FOR RESIDUE RAR A 200
ChainResidue
ALEU5
ASER49
AILE50
ALYS52
ALEU54
APRO55
AARG57
APHE92
ATHR111
ANAP201
AHOH206
AVAL6
AHOH319
AALA7
ALEU20
AASP27
ALEU28
ALYS29
AVAL31
ALYS32

site_idAC2
Number of Residues33
DetailsBINDING SITE FOR RESIDUE NAP A 201
ChainResidue
AVAL6
AALA7
AILE14
AGLY15
AASN18
AGLN19
ALEU20
ATRP22
AGLY43
AARG44
ALYS45
ATHR46
ALEU62
ATHR63
ASER64
AHIS77
AILE79
APHE92
AGLY93
AGLY94
AGLN95
ATHR96
AGLU100
ATHR121
AHOH164
AHOH172
AHOH194
ARAR200
AHOH208
AHOH210
AHOH241
AHOH244
AHOH317

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 202
ChainResidue
AARG12
APRO125
ATYR126
APHE128
AGLU132

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

227111

PDB entries from 2024-11-06

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