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3TYU

Crystal Structure of Dihydropteroate synthetase with Product1

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
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
B0046654biological_processtetrahydrofolate biosynthetic process
B0046656biological_processfolic acid biosynthetic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PT1 A 301
ChainResidue
AASP96
ASER222
AARG255
AHOH294
AHOH297
AASN115
AILE117
AASP185
AGLY189
APHE190
ALEU215
AGLY217
ALYS221

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PT1 B 302
ChainResidue
BASP96
BASN115
BASP185
BGLY189
BPHE190
BGLY217
BLYS221
BSER222
BARG255

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

site_idPS00793
Number of Residues14
DetailsDHPS_2 Dihydropteroate synthase signature 2. GAtLIDIGGesTrP
ChainResidueDetails
AGLY51-PRO64

250059

PDB entries from 2026-03-04

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