Structure of PDB 6tcz Chain L

Receptor sequence
>6tczL (length=202) Species: 5661 (Leishmania donovani) [Search protein sequence]
TTTLAFRFNGGIIVAVDSRASTGQYIASQTVMKVLEINDYLLGTLAGGAA
DCQYWERVLGMECRLWELRNGSRITVAAASKILANITYAYRNHGLSMGTM
VAGWDQFGPSLYYVDDKGSRVKQDLFSVGSGSIYAYGVLDTGYRKDLSVE
DACDLARRSIFHATYRDGASGGIVTVYHVHEKGWTKISRDDQTKLYHRYF
PS
3D structure
PDB6tcz Discovery and Characterization of Clinical Candidate LXE408 as a Kinetoplastid-Selective Proteasome Inhibitor for the Treatment of Leishmaniases.
ChainL
Resolution3.4 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 N2E L T100 G197 Y212 F225 S229 T1 G98 Y113 F126 S130
Gene Ontology
Molecular Function
GO:0004298 threonine-type endopeptidase activity
GO:0008233 peptidase activity
Biological Process
GO:0006508 proteolysis
GO:0051603 proteolysis involved in protein catabolic process
Cellular Component
GO:0000502 proteasome complex
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005839 proteasome core complex

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:6tcz, PDBe:6tcz, PDBj:6tcz
PDBsum6tcz
PubMed32667203
UniProtA0A3Q8IIY4

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