Structure of PDB 6on2 Chain A

Receptor sequence
>6on2A (length=523) Species: 632 (Yersinia pestis) [Search protein sequence]
ALKRKIEAAKMPKDAREKTEAELQKLKMMSPMSAEATVVRGYIDWMLQVP
WNSRSKVKKDLVKAQEVLDTDHYGLERVKDRILEYLAVQSRVSKIKGPIL
CLVGPPGVGKTSLGQSIAKATGRQYVRMALGGVRDEAEIRGHRRTYIGSM
PGKLIQKMAKVGVKNPLFLLDQIDKMASDMRGDPASALLEVLDPEQNVAF
NDHYLEVDYDLSDVMFVATSNSMNIPAPLLDRMEVIRLSGYTEDEKLNIA
KQHLLPKQFERNAIKKGELTIDDSAIMSIIRYYTREAGVRSLEREISKLC
RKAVKNLLMDKTVKHIEINGDNLKDFLGVQKVDYGRADTENRVGQVTGLA
WTEVGGDLLTIETACVPGKGKLTYTGSLGEVMQESIQAALTVVRARADKL
GINPDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVA
MTGEITLRGLVLPIGGLKEKLLAAHRGGIKVVLIPDDNKRDLEEIPDNVI
ADLEIHPVKRIDDVLAIALEHPA
3D structure
PDB6on2 Structural basis for distinct operational modes and protease activation in AAA+ protease Lon.
ChainA
Resolution3.0 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.4.21.53: endopeptidase La.
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 ATP A H324 Y325 P358 G359 V360 G361 K362 T363 S364 Y493 I501 H505 V541 R542 H72 Y73 P106 G107 V108 G109 K110 T111 S112 Y241 I249 H253 V289 R290
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
View graph for
Biological Process
External links
PDB RCSB:6on2, PDBe:6on2, PDBj:6on2
PDBsum6on2
PubMed32490208
UniProtA0A5P8YJ65

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