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2BMB

X-ray structure of the bifunctional 6-hydroxymethyl-7,8- dihydroxypterin pyrophosphokinase dihydropteroate synthase from Saccharomyces cerevisiae

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
A0044237biological_processcellular metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE PMM A1865
ChainResidue
ATHR597
ALYS807
AARG842
AHIS844
AHOH2097
AHOH2115
AARG598
AASP636
AASN655
AILE657
AASP755
APHE760
ALEU801
AGLY803

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PMM A1866
ChainResidue
ASER379
AGLU380
APRO381
AMET382
ATYR383
APHE390
AASN392
AASP434
AARG463
APHE465
AASN698
AHOH2009

Functional Information from PROSITE/UniProt
site_idPS00792
Number of Residues16
DetailsDHPS_1 Dihydropteroate synthase signature 1. ImAIFNaTpDSFsDgG
ChainResidueDetails
AILE546-GLY561

site_idPS00793
Number of Residues14
DetailsDHPS_2 Dihydropteroate synthase signature 2. ESvIIDVGGcsTrP
ChainResidueDetails
AGLU586-PRO599

site_idPS00794
Number of Residues12
DetailsHPPK 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase signature. DnGPRtiDLDIV
ChainResidueDetails
AASP425-VAL436

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P9WND1
ChainResidueDetails
APRO511

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000305|PubMed:15826662, ECO:0007744|PDB:2BMB
ChainResidueDetails
ASER558
APRO615
AILE715
AASN767
ALEU802

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:15826662
ChainResidueDetails
ASER596

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1aj0
ChainResidueDetails
AASN551
AARG598
AARG842

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PDB entries from 2024-07-31

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