Structure of PDB 1fmj Chain A

Receptor sequence
>1fmjA (length=342) Species: 7108 (Spodoptera frugiperda) [Search protein sequence]
PFPYEFRELNPEEDKLVKANLGAFPTTYVKLGPKGYMVYRPYLKDAANIY
NMPLRPTDVFVASYQRSGTTMTQELVWLIENDLNFEAAKTYMSLRYIYLD
GFMIYDPEKQEEYNDILPNPENLDMERYLGLLEYSSRPGSSLLAAVPPTE
KRFVKTHLPLSLMPPNMLDTVKMVYLARDPRDVAVSSFHHARLLYLLNKQ
SNFKDFWEMFHRGLYTLTPYFEHVKEAWAKRHDPNMLFLFYEDYLKDLPG
CIARIADFLGKKLSEEQIQRLCEHLNFEKFKNNGAVNMEDYREIGILADG
EHFIRKGKAGCWRDYFDEEMTKQAEKWIKDNLKDTDLRYPNM
3D structure
PDB1fmj A helical lid converts a sulfotransferase to a dehydratase.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R73 H164 S193
Catalytic site (residue number reindexed from 1) R66 H157 S186
Enzyme Commision number ?
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 CA A E118 N121 D122 E111 N114 D115
BS02 A3P A R73 G75 T76 T77 M78 R185 S193 Y248 F284 F287 R312 K313 G314 R66 G68 T69 T70 M71 R178 S186 Y241 F277 F280 R305 K306 G307
BS03 RTL A Y105 Y120 K162 H164 H197 F310 Y98 Y113 K155 H157 H190 F303
Gene Ontology
Molecular Function
GO:0008146 sulfotransferase activity
GO:0016740 transferase activity
GO:0046872 metal ion binding
Biological Process
GO:0051923 sulfation
Cellular Component
GO:0005737 cytoplasm

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:1fmj, PDBe:1fmj, PDBj:1fmj
PDBsum1fmj
PubMed11323722
UniProtQ26490

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