Structure of PDB 6on2 Chain B Binding Site BS01

Receptor Information
>6on2 Chain B (length=524) Species: 632 (Yersinia pestis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ALKRKIEAAKMPKDAREKTEAELQKLKMMSPMSAEATVVRGYIDWMLQVP
WNSRSKVKKDLVKAQEVLDTDHYGLERVKDRILEYLAVQSRVSKIKGPIL
CLVGPPGVGKTSLGQSIAKATGRQYVRMALGGVRDEAEIRGHRRTYIGSM
PGKLIQKMAKVGVKNPLFLLDQIDKMASDMRGDPASALLEVLDPEQNVAF
NDHYLEVDYDLSDVMFVATSNSMNIPAPLLDRMEVIRLSGYTEDEKLNIA
KQHLLPKQFERNAIKKGELTIDDSAIMSIIRYYTREAGVRSLEREISKLC
RKAVKNLLMDKTVKHIEINGDNLKDFLGVQKVDYGRADTENRVGQVTGLA
WTEVGGDLLTIETACVPGKGKLTYTGSLGEVMQESIQAALTVVRARADKL
GINPDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVA
MTGEITLRGLVLPIGGLKEKLLAAHRGGIKVVLIPDDNKRDLEEIPDNVI
ADLEIHPVKRIDDVLAIALEHPAF
Ligand information
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB6on2 Structural basis for distinct operational modes and protease activation in AAA+ protease Lon.
Resolution3.0 Å
Binding residue
(original residue number in PDB)		Y398 I399
Binding residue
(residue number reindexed from 1)		Y146 I147
Enzymatic activity
Enzyme Commision number 3.4.21.53: endopeptidase La.
Gene Ontology
Molecular Function
GO:0004176 ATP-dependent peptidase activity
GO:0004252 serine-type endopeptidase activity
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
Biological Process
GO:0006508 proteolysis
GO:0030163 protein catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:6on2, PDBe:6on2, PDBj:6on2
PDBsum6on2
PubMed32490208
UniProtA0A5P8YJ65

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