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3CKL

Crystal structure of human cytosolic sulfotransferase SULT1B1 in complex with PAP and resveratrol

Functional Information from GO Data
ChainGOidnamespacecontents
A0004062molecular_functionaryl sulfotransferase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006068biological_processethanol catabolic process
A0006576biological_processbiogenic amine metabolic process
A0006805biological_processxenobiotic metabolic process
A0008146molecular_functionsulfotransferase activity
A0009812biological_processflavonoid metabolic process
A0016740molecular_functiontransferase activity
A0018958biological_processphenol-containing compound metabolic process
A0030855biological_processepithelial cell differentiation
A0042403biological_processthyroid hormone metabolic process
A0050427biological_process3'-phosphoadenosine 5'-phosphosulfate metabolic process
A0051923biological_processsulfation
B0004062molecular_functionaryl sulfotransferase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006068biological_processethanol catabolic process
B0006576biological_processbiogenic amine metabolic process
B0006805biological_processxenobiotic metabolic process
B0008146molecular_functionsulfotransferase activity
B0009812biological_processflavonoid metabolic process
B0016740molecular_functiontransferase activity
B0018958biological_processphenol-containing compound metabolic process
B0030855biological_processepithelial cell differentiation
B0042403biological_processthyroid hormone metabolic process
B0050427biological_process3'-phosphoadenosine 5'-phosphosulfate metabolic process
B0051923biological_processsulfation
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE STL A 501
ChainResidue
ATHR21
APHE24
AMET81
ALEU86
AHIS109
APHE143
AGLN150
ATYR170
ALEU244

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE STL B 501
ChainResidue
BTHR21
BPHE24
BMET81
BHIS109
BPHE143
BASN147
BGLN150
BTYR170
BLEU244

site_idAC3
Number of Residues18
DetailsBINDING SITE FOR RESIDUE A3P A 601
ChainResidue
ALYS48
ASER49
AGLY50
ATHR51
ATHR52
ATRP53
AARG131
ASER139
ATYR194
ATHR228
ASER229
APHE230
AMET233
APHE256
AMET257
AARG258
ALYS259
AGLY260

site_idAC4
Number of Residues18
DetailsBINDING SITE FOR RESIDUE A3P B 601
ChainResidue
BLYS48
BSER49
BGLY50
BTHR51
BTHR52
BTRP53
BARG131
BSER139
BTYR194
BTHR228
BSER229
BPHE230
BMET233
BPHE256
BMET257
BARG258
BLYS259
BGLY260

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
AHIS109
BHIS109

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:16804942, ECO:0000269|Ref.8, ECO:0007744|PDB:2Z5F, ECO:0007744|PDB:3CKL
ChainResidueDetails
ALYS48
BTYR194
BTHR228
BARG258
AARG131
ASER139
ATYR194
ATHR228
AARG258
BLYS48
BARG131
BSER139

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ALYS107
BLYS107

218853

PDB entries from 2024-04-24

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