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5UMG

Crystal structure of dihydropteroate synthase from Klebsiella pneumoniae subsp.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004156molecular_functiondihydropteroate synthase activity
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
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
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue GOL B 301
ChainResidue
BASP185
BGLY217
BLYS221
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. GAtIIDIGGesTrP
ChainResidueDetails
AGLY51-PRO64

222926

PDB entries from 2024-07-24

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