Structure of PDB 1fml Chain A

Receptor sequence
>1fmlA (length=341) Species: 7108 (Spodoptera frugiperda) [Search protein sequence]
LPFPYEFRELNPEEDKLVKANLGAFPTTYVKLGPKGYMVYRPYLKDAANI
YNMPLRPTDVFVASYQRSGTTMTQELVWLIENDLNFEAAKTYMSLRYIYL
DGFMIYDPEKQEEYNDILPNPENLDMERYLGLLEYSSRPGSSLLAAVPPT
EKRFVKTHLPLSLMPPNMLDTVKMVYLARDPRDVAVSSFHHARLLYLLNK
QSNFKDFWEMFHRGLYTLTPYFEHVKEAWAKRHDPNMLFLFYEDYLKDLP
GCIARIADFLGKKLSEEQIQRLCEHLNFEKFKNNGAVNMEDYREIGILAD
GEHFIRKGKAGCWRDYFDEEMTKQAEKWIKDNLKDTDLRYP
3D structure
PDB1fml A helical lid converts a sulfotransferase to a dehydratase.
ChainA
Resolution2.75 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) R67 H158 S187
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 N121 D122 N115 D116
BS02 A3P A R73 S74 G75 T76 T77 M78 R185 S193 Y248 L282 F284 F287 R312 G314 R67 S68 G69 T70 T71 M72 R179 S187 Y242 L276 F278 F281 R306 G308
BS03 RTL A K162 H197 Y298 F310 K156 H191 Y292 F304
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:1fml, PDBe:1fml, PDBj:1fml
PDBsum1fml
PubMed11323722
UniProtQ26490

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