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6E4E

Crystal structure of dihydrofolate reductase from Staphylococcus aureus MW2 bound to NADP and p218

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 Residues30
Detailsbinding site for residue NAP A 201
ChainResidue
AVAL6
ALYS45
ATHR46
ALEU62
ATHR63
ASER64
AILE79
APHE92
AGLY93
AGLY94
AGLN95
AALA7
ATHR96
AGLU100
ATHR121
AMMV202
AHOH305
AHOH310
AHOH315
AHOH320
AHOH347
AHOH362
AILE14
AHOH370
AGLY15
APHE16
AASN18
AGLN19
AGLY43
AARG44

site_idAC2
Number of Residues13
Detailsbinding site for residue MMV A 202
ChainResidue
ALEU5
AVAL6
AALA7
ALEU20
AASP27
ALEU28
AVAL31
ATHR46
ASER49
APHE92
ATHR111
ANAP201
AHOH360

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

224201

PDB entries from 2024-08-28

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