Structure of PDB 2xbn Chain A

Receptor sequence
>2xbnA (length=398) Species: 13689 (Sphingomonas paucimobilis) [Search protein sequence]
RDLLSKFDGLIAERQKLLDSGVTDPFAIVMEQVKSPTEAVIRGKDTILLG
TYNYMGMTFDPDVIAAGKEALEKFGSGTNGSRMLNGTFHDHMEVEQALRD
FYGTTGAIVFSTGYMANLGIISTLAGKGEYVILDADSHASIYDGCQQGNA
EIVRFRHNSVEDLDKRLGRLPKEPAKLVVLEGVYSMLGDIAPLKEMVAVA
KKHGAMVLVDEAHSMGFFGPNGRGVYEAQGLEGQIDFVVGTFSKSVGTVG
GFVVSNHPKFEAVRLACRPYIFTASLPPSVVATATTSIRKLMTAHEKRER
LWSNARALHGGLKAMGFRLGTETCDSAIVAVMLEDQEQAAMMWQALLDGG
LYVNMARPPATPAGTFLLRCSICAEHTPAQIQTVLGMFQAAGRAVGVI
3D structure
PDB2xbn Inhibition of the Plp-Dependent Enzyme Serine Palmitoyltransferase by Cycloserine: Evidence for a Novel Decarboxylative Mechanism of Inactivation.
ChainA
Resolution1.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y73 H159 E202 S206 D231 H234 K265
Catalytic site (residue number reindexed from 1) Y52 H138 E181 S185 D210 H213 K244
Enzyme Commision number 2.3.1.50: serine C-palmitoyltransferase.
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 PMP A G134 Y135 H159 D231 T262 S264 K265 G113 Y114 H138 D210 T241 S243 K244
Gene Ontology
Molecular Function
GO:0016740 transferase activity
GO:0016746 acyltransferase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0006629 lipid metabolic process
GO:0006665 sphingolipid metabolic process
GO:0009058 biosynthetic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Cellular Component
External links
PDB RCSB:2xbn, PDBe:2xbn, PDBj:2xbn
PDBsum2xbn
PubMed20445930
UniProtQ93UV0|SPT_SPHPI Serine palmitoyltransferase (Gene Name=spt)

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