Structure of PDB 5lnq Chain B

Receptor sequence
>5lnqB (length=430) Species: 5665 (Leishmania mexicana) [Search protein sequence]
ASRVFIVGGHITPFVGKGSPLFIDKKHPDFGKKKNMTLEEILATTVQGTM
EHSGLSGREGIVDQVVVGNFLGELFSSQGHLGPAAIGSLTYGQAGSKNPL
MYKPAMRVEGAAASGGLAVISAMNALKSGSADITLAVGVEVQTTASARVG
GDYLARAADYQRQRQLDDFTFPCLFAKRMKYIAEHNHFTMEDTARVAAKA
YANGNKNPLAHMHTRKLTFEQCNGEDPSNVKFLGNETYKEYLRMTDCSQV
SDGGAGVVLANEEGLRKMGLSPNDSRLVEIKSIACAVSNLYEDPDDACCM
FTSRQAAQKALSMANIKPSDLNVAEVHDCFTIAEMLMYEALGIAEYGHAK
DLIRNGDTTLEGRIPVNTGGGLLSFGHPVGATGIKQIMEVYRQMKGQCEA
YQMKKIPALGATLNMGGDDKTAVSAVLQNI
3D structure
PDB5lnq Crystallographic substrate binding studies of Leishmania mexicana SCP2-thiolase (type-2): unique features of oxyanion hole-1.
ChainB
Resolution1.98 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) A123
Catalytic site (residue number reindexed from 1) A112
Enzyme Commision number 2.3.1.176: propanoyl-CoA C-acyltransferase.
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 CAA B K28 A123 R159 L165 A168 F182 P183 V241 C258 S259 V261 H388 G428 K17 A112 R148 L154 A157 F171 P172 V230 C247 S248 V250 H377 G417
Gene Ontology
Molecular Function
GO:0003988 acetyl-CoA C-acyltransferase activity
GO:0008289 lipid binding
GO:0016746 acyltransferase activity
GO:0016747 acyltransferase activity, transferring groups other than amino-acyl groups
Biological Process
GO:0006869 lipid transport
Cellular Component
GO:0005777 peroxisome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5lnq, PDBe:5lnq, PDBj:5lnq
PDBsum5lnq
PubMed28062645
UniProtE9AW84

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