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5USW

The crystal structure of 7,8-dihydropteroate synthase from Vibrio fischeri ES114

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
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
B0046872molecular_functionmetal ion binding
C0004156molecular_functiondihydropteroate synthase activity
C0005829cellular_componentcytosol
C0009396biological_processfolic acid-containing compound biosynthetic process
C0016740molecular_functiontransferase activity
C0042558biological_processpteridine-containing compound metabolic process
C0044237biological_processcellular metabolic process
C0046654biological_processtetrahydrofolate biosynthetic process
C0046656biological_processfolic acid biosynthetic process
C0046872molecular_functionmetal ion binding
D0004156molecular_functiondihydropteroate synthase activity
D0005829cellular_componentcytosol
D0009396biological_processfolic acid-containing compound biosynthetic process
D0016740molecular_functiontransferase activity
D0042558biological_processpteridine-containing compound metabolic process
D0044237biological_processcellular metabolic process
D0046654biological_processtetrahydrofolate biosynthetic process
D0046656biological_processfolic acid biosynthetic process
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue GOL A 301
ChainResidue
AHIS140
AGLN142
ALEU157
AILE161
APRO186
ALYS192
AHIS196
AHOH479

site_idAC2
Number of Residues4
Detailsbinding site for residue GOL A 302
ChainResidue
AARG88
APHE89
AHOH474
AGLU45

site_idAC3
Number of Residues7
Detailsbinding site for residue GOL A 303
ChainResidue
AASN115
AVAL117
AASP185
APHE190
ALYS221
AHOH425
AHOH428

site_idAC4
Number of Residues2
Detailsbinding site for residue FMT A 304
ChainResidue
AASN7
AHOH513

site_idAC5
Number of Residues5
Detailsbinding site for residue ACT A 305
ChainResidue
AARG220
APRO232
ALYS233
ALEU236
AASP258

site_idAC6
Number of Residues8
Detailsbinding site for residue GOL B 301
ChainResidue
BHIS140
BGLN142
BLEU157
BILE161
BPRO186
BLYS192
BHIS196
BHOH449

site_idAC7
Number of Residues1
Detailsbinding site for residue GOL B 302
ChainResidue
BGLN252

site_idAC8
Number of Residues6
Detailsbinding site for residue FMT B 303
ChainResidue
BMSE139
BASP185
BLYS221
BARG255
BHOH438
BHOH572

site_idAC9
Number of Residues5
Detailsbinding site for residue FMT B 304
ChainResidue
BLYS8
BHIS86
BPHE89
BASP90
BHOH460

site_idAD1
Number of Residues2
Detailsbinding site for residue FMT B 305
ChainResidue
BLYS192
BHOH419

site_idAD2
Number of Residues8
Detailsbinding site for residue GOL C 301
ChainResidue
CHIS140
CGLN142
CLEU157
CILE161
CPRO186
CLYS192
CHIS196
CHOH459

site_idAD3
Number of Residues8
Detailsbinding site for residue GOL C 302
ChainResidue
CASN115
CVAL117
CASP185
CPHE190
CLYS221
CARG255
CHOH416
CHOH418

site_idAD4
Number of Residues8
Detailsbinding site for residue GOL D 301
ChainResidue
DHIS140
DGLN142
DLEU157
DILE161
DPRO186
DLYS192
DHIS196
DHOH426

site_idAD5
Number of Residues10
Detailsbinding site for residue GOL D 302
ChainResidue
DASN115
DVAL117
DASP185
DPHE190
DLYS221
DARG255
DHOH405
DHOH410
DHOH412
DHOH416

Functional Information from PROSITE/UniProt
site_idPS00792
Number of Residues16
DetailsDHPS_1 Dihydropteroate synthase signature 1. VmGILNvTpDSFsDgG
ChainResidueDetails
AVAL17-GLY32

223166

PDB entries from 2024-07-31

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