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1EYE

1.7 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF 6-HYDROXYMETHYL-7,8-DIHYDROPTEROATE SYNTHASE (DHPS) FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH 6-HYDROXYMETHYLPTERIN MONOPHOSPHATE

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
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 300
ChainResidue
AASN13
AGLY22
AHIS255
APMM301

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE PMM A 301
ChainResidue
AMET130
AASP177
APHE182
AGLY209
ALYS213
AARG253
AHIS255
AMG300
AHOH302
AHOH303
AHOH306
AHOH307
AHOH308
AASN13
AASP21
AASP86
AASN105
AVAL107

Functional Information from PROSITE/UniProt
site_idPS00792
Number of Residues16
DetailsDHPS_1 Dihydropteroate synthase signature 1. VmGVLNvTdDSFsDgG
ChainResidueDetails
AVAL8-GLY23

site_idPS00793
Number of Residues14
DetailsDHPS_2 Dihydropteroate synthase signature 2. GAgIVDVGGesSrP
ChainResidueDetails
AGLY42-PRO55

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11007651","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11007651","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1EYE","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1aj0
ChainResidueDetails
AASN13
AARG253

246704

PDB entries from 2025-12-24

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