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5VIS

1.73 Angstrom Resolution Crystal Structure of Dihydropteroate Synthase (folP-SMZ_B27) from Soil Uncultured Bacterium.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004156molecular_functiondihydropteroate synthase activity
A0009396biological_processfolic acid-containing compound biosynthetic process
A0042558biological_processpteridine-containing compound metabolic process
A0044237biological_processcellular metabolic process
B0004156molecular_functiondihydropteroate synthase activity
B0009396biological_processfolic acid-containing compound biosynthetic process
B0042558biological_processpteridine-containing compound metabolic process
B0044237biological_processcellular metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue MLA A 301
ChainResidue
ALYS225
BHOH410
BHOH478
BHOH501
ATHR226
AARG229
AHOH450
AHOH609
BLYS225
BTHR226
BARG229
BTAR303

site_idAC2
Number of Residues2
Detailsbinding site for residue CL B 301
ChainResidue
BVAL147
BVAL147

site_idAC3
Number of Residues7
Detailsbinding site for residue K B 302
ChainResidue
BGLU49
BASP86
BHOH447
BHOH509
BHOH513
BHOH579
BHOH622

site_idAC4
Number of Residues13
Detailsbinding site for residue TAR B 303
ChainResidue
ALYS225
AARG229
AMLA301
AHOH609
BPHE141
BHIS182
BSER216
BARG229
BHOH402
BHOH406
BHOH410
BHOH501
BHOH623

site_idAC5
Number of Residues5
Detailsbinding site for residue GOL B 304
ChainResidue
BMET1
BSER199
BGLN202
BLEU242
BHOH570

Functional Information from PROSITE/UniProt
site_idPS00792
Number of Residues16
DetailsDHPS_1 Dihydropteroate synthase signature 1. IvGILNvTpNSFhDgG
ChainResidueDetails
AILE6-GLY21

219140

PDB entries from 2024-05-01

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