Structure of PDB 5lnq Chain D

Receptor sequence
>5lnqD (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.
ChainD
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 D A123 L165 P183 F186 V241 S259 V261 H338 C340 H388 M426 G428 A112 L154 P172 F175 V230 S248 V250 H327 C329 H377 M415 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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