Structure of PDB 5z9o Chain A

Receptor sequence
>5z9oA (length=373) Species: 272621 (Lactobacillus acidophilus NCFM) [Search protein sequence]
LEKTFYKMMLSKSFPFPVEVTYWDGKSEVYGNGTPEIHITFNEKIPMSDI
TKNASLALGEAYMDKKIEIQGSIQELINGAYQSADSFMRSSKFRKSHYDI
GNDFYKLWLDPTMTYSCAYFTDDNKDDLEQAQIAKVHHILNKLHPEKGKT
LLDIGCGWGTLMLTAAKEYGLKVTGVTLSEEQYKLVQKKIYDEGLEDVAE
VKLEDYRELGDQQWDYVTSVGMFEHVGSENLGEYFKDVAKYLKNDGVALI
HGITRQQGGATNAWINKYIFPGGYIPGLVEIISRIEEANLQVSDVEMLRR
HYQRTLEIWDKNFNNARPEIEKNMGERFCRMWDLYLQACAASFESGNIDV
VQYLLTKGPSGKSLPMTRKYMLN
3D structure
PDB5z9o Crystal structure of bacterial cyclopropane-fatty-acyl-phospholipid synthase with phospholipid.
ChainA
Resolution2.7 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.1.1.79: cyclopropane-fatty-acyl-phospholipid synthase.
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 CO3 A S134 C135 H269 Y320 S116 C117 H251 Y302
BS02 EPH A Y82 E242 H243 I271 A278 N280 I283 F288 G291 I293 Y320 Y353 A356 C357 S360 I366 Y81 E224 H225 I253 A260 N262 I265 F270 G273 I275 Y302 Y335 A338 C339 S342 I348
Gene Ontology
Molecular Function
GO:0008168 methyltransferase activity
GO:0008825 cyclopropane-fatty-acyl-phospholipid synthase activity
Biological Process
GO:0006629 lipid metabolic process
GO:0008610 lipid biosynthetic process
GO:0032259 methylation

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Molecular Function
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Biological Process
External links
PDB RCSB:5z9o, PDBe:5z9o, PDBj:5z9o
PDBsum5z9o
PubMed30828715
UniProtQ5FJM0

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