Structure of PDB 6on2 Chain F

Receptor sequence
>6on2F (length=512) Species: 632 (Yersinia pestis) [Search protein sequence]
ALKRKIEAAKMPKDAREKTEAELQKLKMMSPMSAEATVVRGYIDWMLQVP
WNSRSKVKKDLVKAQEVLDTDHYGLERVKDRILEYLAVQSRVSKIKGPIL
CLVGPPGVGKTSLGQSIAKATGRQYVRMALGRRTYIGSMPGKLIQKMAKV
GVKNPLFLLDQIDKMASDMRGDPASALLEVLDPEQNVAFNDHYLEVDYDL
SDVMFVATSNSMNIPAPLLDRMEVIRLSGYTEDEKLNIAKQHLLPKQFER
NAIKKGELTIDDSAIMSIIRYYTREAGVRSLEREISKLCRKAVKNLLMDK
TVKHIEINGDNLKDFLGVQKVDYGRADTENRVGQVTGLAWTEVGGDLLTI
ETACVPGKGKLTYTGSLGEVMQESIQAALTVVRARADKLGINPDFYEKRD
IHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGLV
LPIGGLKEKLLAAHRGGIKVVLIPDDNKRDLEEIPDNVIADLEIHPVKRI
DDVLAIALEHPA
3D structure
PDB6on2 Structural basis for distinct operational modes and protease activation in AAA+ protease Lon.
ChainF
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 ADP F H324 Y325 G359 V360 G361 K362 T363 Y493 I501 H505 V541 R542 H72 Y73 G107 V108 G109 K110 T111 Y230 I238 H242 V278 R279
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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