Structure of PDB 6v11 Chain E

Receptor sequence
>6v11E (length=464) Species: 632 (Yersinia pestis) [Search protein sequence]
ALKRKIEAAKMPKDAREKTEAELQKLKMMSPMSAEATVVRGYIDWMLQAQ
EVLDTDHYGLERVKDRILEYLAVQSRVSKIKGPILCLVGPPGVGKTSLGQ
SIAKATGRQYVRMALGPGKLIQKMAKVGVKNPLFLLDEIDKASALLEVLD
PEQSDVMFVATSNSMNIPAPLLDRMEVIRLSGYTEDEKLNIAKQHLLPKQ
FERNAIKKGELTIDDSAIMSIIRYYTREAGVRSLEREISKLCRKAVKNLL
MDKTVKHIEINGDNLKDFLGVQKVDGRADTENRVGQVTGLAWTEVGGDLL
TIETACVPGKGKLTYTGSLGEVMQESIQAALTVVRARADKLGINPDFYEK
RDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRG
LVLPIGGLKEKLLAAHRGGIKVVLIPDDNKRDLEEIPDNVIADLEIHPVK
RIDDVLAIALEHPA
3D structure
PDB6v11 Structural basis for distinct operational modes and protease activation in AAA+ protease Lon.
ChainE
Resolution3.8 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 E H324 Y325 V360 G361 T363 S364 Y493 I501 V541 R542 H57 Y58 V93 G94 T96 S97 Y183 I191 V231 R232
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:6v11, PDBe:6v11, PDBj:6v11
PDBsum6v11
PubMed32490208
UniProtA0A5P8YJ65

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