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1Z29

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
A0009309biological_processamine biosynthetic process
A0016740molecular_functiontransferase activity
A0018958biological_processphenol-containing compound metabolic process
A0047894molecular_functionflavonol 3-sulfotransferase activity
A0050427biological_process3'-phosphoadenosine 5'-phosphosulfate metabolic process
A0051923biological_processsulfation
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 1010
ChainResidue
ALYS106
ATYR240
AACY721
AHOH2057

site_idAC2
Number of Residues22
DetailsBINDING SITE FOR RESIDUE A3P A 2001
ChainResidue
ATRP53
AARG130
ASER138
ATYR193
ATHR227
ASER228
APHE229
AMET232
APHE255
AMET256
AARG257
ALYS258
AGLY259
AHOH2005
AHOH2012
AHOH2013
AHOH2025
ALYS48
ASER49
AGLY50
ATHR51
ATHR52

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACY A 721
ChainResidue
APHE81
ALYS106
AHIS108
ATYR149
ACA1010
AHOH2011

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 Residues6
DetailsBINDING:
ChainResidueDetails
ALYS48
AARG130
ASER138
ATYR193
ATHR227
APHE255

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ALYS106

224572

PDB entries from 2024-09-04

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