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1AD1

DIHYDROPTEROATE SYNTHETASE (APO FORM) FROM STAPHYLOCOCCUS AUREUS

Functional Information from GO Data
ChainGOidnamespacecontents
A0004156molecular_functiondihydropteroate synthase activity
A0005829cellular_componentcytosol
A0009396biological_processfolic acid-containing compound biosynthetic process
A0016740molecular_functiontransferase activity
A0042558biological_processpteridine-containing compound metabolic process
A0044237biological_processcellular metabolic process
A0046654biological_processtetrahydrofolate biosynthetic process
A0046656biological_processfolic acid biosynthetic process
A0046677biological_processresponse to antibiotic
A0046872molecular_functionmetal ion binding
B0004156molecular_functiondihydropteroate synthase activity
B0005829cellular_componentcytosol
B0009396biological_processfolic acid-containing compound biosynthetic process
B0016740molecular_functiontransferase activity
B0042558biological_processpteridine-containing compound metabolic process
B0044237biological_processcellular metabolic process
B0046654biological_processtetrahydrofolate biosynthetic process
B0046656biological_processfolic acid biosynthetic process
B0046677biological_processresponse to antibiotic
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE K B 1
ChainResidue
BVAL75
BPHE77
BVAL79
BHOH291

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K A 268
ChainResidue
AVAL75
APHE77
AVAL79
AHOH517
AHOH589

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE TRS A 500
ChainResidue
ALYS96

Functional Information from PROSITE/UniProt
site_idPS00792
Number of Residues16
DetailsDHPS_1 Dihydropteroate synthase signature 1. ImGILNvTpDSFsDgG
ChainResidueDetails
AILE6-GLY21

site_idPS00793
Number of Residues14
DetailsDHPS_2 Dihydropteroate synthase signature 2. GAdIIDVGGvsTrP
ChainResidueDetails
AGLY40-PRO53

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:9149138
ChainResidueDetails
AASN11
BASN11

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000305|PubMed:9149138, ECO:0007744|PDB:1AD4
ChainResidueDetails
AARG52
BASP167
BLYS203
BARG239
AASP84
AASN103
AASP167
ALYS203
AARG239
BARG52
BASP84
BASN103

218853

PDB entries from 2024-04-24

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