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2A3R

Crystal Structure of Human Sulfotransferase SULT1A3 in Complex with Dopamine and 3-Phosphoadenosine 5-Phosphate

Functional Information from GO Data
ChainGOidnamespacecontents
A0004062molecular_functionaryl sulfotransferase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006068biological_processethanol catabolic process
A0006584biological_processcatecholamine metabolic process
A0006805biological_processxenobiotic metabolic process
A0008146molecular_functionsulfotransferase activity
A0008202biological_processsteroid metabolic process
A0009812biological_processflavonoid metabolic process
A0016740molecular_functiontransferase activity
A0042417biological_processdopamine metabolic process
A0042420biological_processdopamine catabolic process
A0043199molecular_functionsulfate binding
A0047685molecular_functionamine sulfotransferase activity
A0050427biological_process3'-phosphoadenosine 5'-phosphosulfate metabolic process
A0051923biological_processsulfation
A1903351biological_processcellular response to dopamine
B0004062molecular_functionaryl sulfotransferase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006068biological_processethanol catabolic process
B0006584biological_processcatecholamine metabolic process
B0006805biological_processxenobiotic metabolic process
B0008146molecular_functionsulfotransferase activity
B0008202biological_processsteroid metabolic process
B0009812biological_processflavonoid metabolic process
B0016740molecular_functiontransferase activity
B0042417biological_processdopamine metabolic process
B0042420biological_processdopamine catabolic process
B0043199molecular_functionsulfate binding
B0047685molecular_functionamine sulfotransferase activity
B0050427biological_process3'-phosphoadenosine 5'-phosphosulfate metabolic process
B0051923biological_processsulfation
B1903351biological_processcellular response to dopamine
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE A3P A 296
ChainResidue
ALYS48
ATHR227
ASER228
APHE229
AMET232
APHE255
AMET256
AARG257
ALYS258
AGLY259
AHOH310
ASER49
AHOH313
AHOH317
AHOH343
AGLY50
ATHR51
ATHR52
ATRP53
AARG130
ASER138
ATYR193

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE LDP A 297
ChainResidue
APHE24
APRO47
APHE81
AASP86
ALYS106
AHIS108
AGLU146
AALA148
AHIS149

site_idAC3
Number of Residues22
DetailsBINDING SITE FOR RESIDUE A3P B 296
ChainResidue
BLYS48
BSER49
BGLY50
BTHR51
BTHR52
BTRP53
BARG130
BSER138
BTYR193
BTHR227
BSER228
BPHE229
BMET232
BPHE255
BMET256
BARG257
BLYS258
BGLY259
BHOH300
BHOH309
BHOH316
BHOH333

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE LDP B 297
ChainResidue
BPHE24
BPRO47
BPHE81
BASP86
BLYS106
BHIS108
BGLU146
BALA148
BHIS149

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P49888
ChainResidueDetails
AHIS108
BHIS108

site_idSWS_FT_FI2
Number of Residues18
DetailsBINDING: BINDING => ECO:0000269|PubMed:16083857, ECO:0007744|PDB:2A3R
ChainResidueDetails
ALYS48
BLYS48
BASP86
BLYS106
BARG130
BSER138
BGLU146
BTYR193
BTHR227
BARG257
AASP86
ALYS106
AARG130
ASER138
AGLU146
ATYR193
ATHR227
AARG257

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PDB entries from 2024-10-09

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