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8TU9

Cryo-EM structure of HGSNAT-acetyl-CoA complex at pH 7.5

Functional Information from GO Data
ChainGOidnamespacecontents
A0003674molecular_functionmolecular_function
A0005575cellular_componentcellular_component
A0005764cellular_componentlysosome
A0005765cellular_componentlysosomal membrane
A0005886cellular_componentplasma membrane
A0006091biological_processgeneration of precursor metabolites and energy
A0007041biological_processlysosomal transport
A0008218biological_processbioluminescence
A0015019molecular_functionheparan-alpha-glucosaminide N-acetyltransferase activity
A0016020cellular_componentmembrane
A0016746molecular_functionacyltransferase activity
A0030200biological_processheparan sulfate proteoglycan catabolic process
A0035579cellular_componentspecific granule membrane
A0043202cellular_componentlysosomal lumen
A0051259biological_processprotein complex oligomerization
A0070821cellular_componenttertiary granule membrane
B0003674molecular_functionmolecular_function
B0005575cellular_componentcellular_component
B0005764cellular_componentlysosome
B0005765cellular_componentlysosomal membrane
B0005886cellular_componentplasma membrane
B0006091biological_processgeneration of precursor metabolites and energy
B0007041biological_processlysosomal transport
B0008218biological_processbioluminescence
B0015019molecular_functionheparan-alpha-glucosaminide N-acetyltransferase activity
B0016020cellular_componentmembrane
B0016746molecular_functionacyltransferase activity
B0030200biological_processheparan sulfate proteoglycan catabolic process
B0035579cellular_componentspecific granule membrane
B0043202cellular_componentlysosomal lumen
B0051259biological_processprotein complex oligomerization
B0070821cellular_componenttertiary granule membrane
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues584
DetailsTOPO_DOM: Lumenal, vesicle => ECO:0000255
ChainResidueDetails
AMET1-ASP190
BILE442-THR500
BPHE551-LYS564
BVAL614-LYS634
AMET297-GLN302
AALA367-CYS374
AILE442-THR500
APHE551-LYS564
AVAL614-LYS634
BMET1-ASP190
BMET297-GLN302
BALA367-CYS374

site_idSWS_FT_FI2
Number of Residues400
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
AASP191-SER211
APHE593-ILE613
BASP191-SER211
BTHR276-SER296
BARG303-CYS323
BPRO346-PHE366
BALA375-LEU395
BGLY421-TYR441
BLYS501-LEU521
BPHE530-ALA550
BGLY565-GLY585
ATHR276-SER296
BPHE593-ILE613
AARG303-CYS323
APRO346-PHE366
AALA375-LEU395
AGLY421-TYR441
ALYS501-LEU521
APHE530-ALA550
AGLY565-GLY585

site_idSWS_FT_FI3
Number of Residues242
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
AGLU212-LEU275
BHIS586-TYR592
AILE324-ILE345
AILE396-LEU420
ATHR522-GLY529
AHIS586-TYR592
BGLU212-LEU275
BILE324-ILE345
BILE396-LEU420
BTHR522-GLY529

site_idSWS_FT_FI4
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:20650889
ChainResidueDetails
AMET297
BMET297

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
AVAL243
BVAL243

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR245
BTHR245

site_idSWS_FT_FI7
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AGLY94
ASER162
BGLY94
BSER162

site_idSWS_FT_FI8
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218
ChainResidueDetails
AILE142
BILE142

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: (Z)-2,3-didehydrotyrosine => ECO:0000269|PubMed:8448132
ChainResidueDetails
ATYR-190
BTYR-190

site_idSWS_FT_FI10
Number of Residues4
DetailsCROSSLNK: 5-imidazolinone (Ser-Gly) => ECO:0000269|PubMed:8448132
ChainResidueDetails
ATHR-191
AGLY-189
BTHR-191
BGLY-189

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PDB entries from 2024-07-17

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