Structure of PDB 3a2b Chain A

Receptor sequence
>3a2bA (length=392) Species: 28454 (Sphingobacterium multivorum) [Search protein sequence]
SKGKLGEKISQFKIVEELKAKGLYAYFRPIQSKQDTEVKIDGRRVLMFGS
NSYLGLTTDTRIIKAAQDALEKYGTGCAGSRFLNGTLDIHVELEEKLSAY
VGKEAAILFSTGFQSNLGPLSCLMGRNDYILLDERDHASIIDGSRLSFSK
VIKYGHNNMEDLRAKLSRLPEDSAKLICTDGIFSMEGDIVNLPELTSIAN
EFDAAVMVDDAHSLGVIGHKGAGTASHFGLNDDVDLIMGTFSKSLASLGG
FVAGDADVIDFLKHNARSVMFSASMTPASVASTLKALEIIQNEPEHIEKL
WKNTDYAKAQLLDHGFDLGATESPILPIFIRSNEKTFWVTKMLQDDGVFV
NPVVSPAVPAEESLIRFSLMATHTYDQIDEAIEKMVKVFKQA
3D structure
PDB3a2b Structural Insights into the Enzymatic Mechanism of Serine Palmitoyltransferase from Sphingobacterium multivorum
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N52 H138 D181 S185 D210 H213 K244
Catalytic site (residue number reindexed from 1) N51 H137 D180 S184 D209 H212 K243
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 SER A H138 K244 H137 K243
BS02 PLP A G113 F114 H138 D210 A212 H213 T241 S243 K244 G112 F113 H137 D209 A211 H212 T240 S242 K243
Gene Ontology
Molecular Function
GO:0004758 serine C-palmitoyltransferase activity
GO:0008710 8-amino-7-oxononanoate synthase activity
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
GO:0005886 plasma membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3a2b, PDBe:3a2b, PDBj:3a2b
PDBsum3a2b
PubMed19564159
UniProtA7BFV6|SPT_SPHMU Serine palmitoyltransferase (Gene Name=spt)

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