Structure of PDB 5eue Chain B

Receptor sequence
>5eueB (length=449) Species: 292459 (Symbiobacterium thermophilum IAM 14863) [Search protein sequence]
YRDRFPSHARLPRAGLPRAEILAEIAAMGAAESPAWRDGYASGAVYHGDE
HHIAFLNEVYALQSQSNPLHPDLWPSTAKFEAEVVAMTAHMLGGDAAGGT
VCGTVTSGGTESLLLAMKTYRDWARATKGITAPEAVVPVSAHAAFDKAAQ
YFGIKLVRTPLDADYRADVAAMREAITPNTVVVAGSAPGFPHGVVDPIPE
IAALAAEHGIGCHVDACLGGFILPWAERLGYPVPPFDFRLEGVTSVSADT
HKYGYGAKGTSVILYRRPDLLHYQYFIAADWPGGIYASPTFAGSRPGALS
ATAWAAMLSLGEEGYLDATRRILQAADRLKAGVRAIPSLKILGDPLWVIA
VASDELNIYQVMEEMAGRGWRLNGLHRPPAFHVALTLRHTEPGVVDRFLA
DLQDAVAQVRAHPEKATGMAPVYGMAAAAPPELVRQVSTGFIDLLYEVH
3D structure
PDB5eue Creation of a S1P Lyase bacterial surrogate for structure-based drug design.
ChainB
Resolution2.83 Å
3D
structure
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Enzymatic activity
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 5S5 B N432 V496 F500 N373 V437 F441 PDBbind-CN: -logKd/Ki=6.77,IC50=0.17uM
BS02 5S5 B L128 P130 I344 Y345 A346 L69 P71 I285 Y286 A287 PDBbind-CN: -logKd/Ki=6.77,IC50=0.17uM
Gene Ontology
Molecular Function
GO:0004058 aromatic-L-amino-acid decarboxylase activity
GO:0008117 sphinganine-1-phosphate aldolase activity
GO:0016829 lyase activity
GO:0016830 carbon-carbon lyase activity
GO:0030170 pyridoxal phosphate binding
GO:0042802 identical protein binding
Biological Process
GO:0019752 carboxylic acid metabolic process
GO:0030149 sphingolipid catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:5eue, PDBe:5eue, PDBj:5eue
PDBsum5eue
PubMed27013389
UniProtQ67PY4

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