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1Z28

Crystal Structures of SULT1A2 and SULT1A1*3: Implications in the bioactivation of N-hydroxy-2-acetylamino fluorine (OH-AAF)

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
A0008210biological_processestrogen metabolic process
A0009308biological_processamine metabolic process
A0009812biological_processflavonoid metabolic process
A0016740molecular_functiontransferase activity
A0047894molecular_functionflavonol 3-sulfotransferase activity
A0050294molecular_functionsteroid sulfotransferase activity
A0050427biological_process3'-phosphoadenosine 5'-phosphosulfate metabolic process
A0050656molecular_function3'-phosphoadenosine 5'-phosphosulfate binding
A0051923biological_processsulfation
Functional Information from PDB Data
site_idAC1
Number of Residues23
DetailsBINDING SITE FOR RESIDUE A3P A 1001
ChainResidue
ALYS48
ATHR227
ASER228
APHE229
AMET232
APHE255
AMET256
AARG257
ALYS258
AGLY259
AHOH1005
ASER49
AHOH1014
AHOH1015
AHOH1031
AHOH1045
AGLY50
ATHR51
ATHR52
ATRP53
AARG130
ASER138
ATYR193

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
AHIS108

site_idSWS_FT_FI2
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:12471039, ECO:0000269|PubMed:16221673
ChainResidueDetails
ALYS48
ALYS106
AARG130
ASER138
ATYR193
ATHR227
APHE255

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P17988
ChainResidueDetails
ASER138

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PDB entries from 2024-07-31

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