Structure of PDB 1z29 Chain A

Receptor sequence
>1z29A (length=281) Species: 9606 (Homo sapiens) [Search protein sequence]
SRPPLEYVKGVPLIKYFAEALGPLQSFQARPDDLLISTYPKSGTTWVSQI
LDMIYQGGAPIFMRVPFLEFKVPGIPSGMETLKNTPAPRLLKTHLPLALL
PQTLLDQKVKVVYVARNAKDVAVSYYHFYHMAKVYPHPGTWESFLEKFMA
GEVSYGSWYQHVQEWWELSRTHPVLYLFYEDMKENPKREIQKILEFVGRS
LPEETVDLMVEHTSFKEMKKNPMTNYTTVRREFMDHSISPFMRKGMAGDW
KTTFTVAQNERFDADYAEKMAGCSLSFRSEL
3D structure
PDB1z29 Crystal structures of SULT1A2 and SULT1A1 *3: insights into the substrate inhibition and the role of Tyr149 in SULT1A2.
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K48 H108 S138
Catalytic site (residue number reindexed from 1) K41 H94 S124
Enzyme Commision number 2.8.2.1: aryl sulfotransferase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 A3P A K48 G50 T51 T52 W53 R130 S138 Y193 F229 F255 M256 R257 K258 G259 K41 G43 T44 T45 W46 R116 S124 Y179 F215 F241 M242 R243 K244 G245
Gene Ontology
Molecular Function
GO:0004062 aryl sulfotransferase activity
GO:0005515 protein binding
GO:0008146 sulfotransferase activity
GO:0016740 transferase activity
GO:0047894 flavonol 3-sulfotransferase activity
Biological Process
GO:0006068 ethanol catabolic process
GO:0006584 catecholamine metabolic process
GO:0006805 xenobiotic metabolic process
GO:0008202 steroid metabolic process
GO:0009309 amine biosynthetic process
GO:0018958 phenol-containing compound metabolic process
GO:0050427 3'-phosphoadenosine 5'-phosphosulfate metabolic process
GO:0051923 sulfation
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:1z29, PDBe:1z29, PDBj:1z29
PDBsum1z29
PubMed20417180
UniProtP50226|ST1A2_HUMAN Sulfotransferase 1A2 (Gene Name=SULT1A2)

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