Structure of PDB 6td5 Chain l

Receptor sequence
>6td5l (length=201) Species: 5661 (Leishmania donovani) [Search protein sequence]
TTTLAFRFNGGIIVAVDSRASTGQYIASQTVMKVLEINDYLLGTLAGGAA
DCQYWERVLGMECRLWELRNGSRITVAAASKILANITYAYRNHGLSMGTM
VAGWDQFGPSLYYVDDKGSRVKQDLFSVGSGSIYAYGVLDTGYRKDLSVE
DACDLARRSIFHATYRDGASGGIVTVYHVHEKGWTKISRDDQTKLYHRYF
P
3D structure
PDB6td5 Discovery and Characterization of Clinical Candidate LXE408 as a Kinetoplastid-Selective Proteasome Inhibitor for the Treatment of Leishmaniases.
Chainl
Resolution3.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T100 D116 R118 K132 G146 S229 D266 S269
Catalytic site (residue number reindexed from 1) T1 D17 R19 K33 G47 S130 D167 S170
Enzyme Commision number 3.4.25.1: proteasome endopeptidase complex.
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 BO2 l T100 A119 S120 T121 L144 G146 A148 T1 A20 S21 T22 L45 G47 A49
BS02 N2E l S120 G122 Y212 V227 G228 S229 Y235 S21 G23 Y113 V128 G129 S130 Y136
Gene Ontology
Molecular Function
GO:0004298 threonine-type endopeptidase activity
Biological Process
GO:0051603 proteolysis involved in protein catabolic process
Cellular Component
GO:0005839 proteasome core complex

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Cellular Component
External links
PDB RCSB:6td5, PDBe:6td5, PDBj:6td5
PDBsum6td5
PubMed32667203
UniProtA0A3Q8IIY4

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