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3MCN

Crystal Structure of the 6-hyroxymethyl-7,8-dihydropterin pyrophosphokinase dihydropteroate synthase bifunctional enzyme from Francisella tularensis

Functional Information from GO Data
ChainGOidnamespacecontents
A0003848molecular_function2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity
A0004156molecular_functiondihydropteroate synthase activity
A0009396biological_processfolic acid-containing compound biosynthetic process
A0042558biological_processpteridine-containing compound metabolic process
B0003848molecular_function2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity
B0004156molecular_functiondihydropteroate synthase activity
B0009396biological_processfolic acid-containing compound biosynthetic process
B0042558biological_processpteridine-containing compound metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG A 423
ChainResidue
AASP101
AASP103

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE B57 B 423
ChainResidue
BASP255
BASN277
BILE301
BASP346
BLYS383
BARG418

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE B57 B 424
ChainResidue
BPHE59
BASN61
BASP101
BPHE129
BMG425
BHOH496
BGLY9

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 425
ChainResidue
BGLY7
BASP101
BASP103
BB57424
BHOH460

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG B 426
ChainResidue
BGLU83
BASP101
BLEU102
BASP103

Functional Information from PROSITE/UniProt
site_idPS00793
Number of Residues14
DetailsDHPS_2 Dihydropteroate synthase signature 2. GAeIIDIGAesTkP
ChainResidueDetails
AGLY205-PRO218

237735

PDB entries from 2025-06-18

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