Structure of PDB 6v11 Chain B

Receptor sequence
>6v11B (length=496) Species: 632 (Yersinia pestis) [Search protein sequence]
ALKRKIEAAKMPKDAREKTEAELQKLKMMSPMSAEATVVRGYIDWMLQVP
WNSRSKVKKDLVKAQEVLDTDHYGLERVKDRILEYLAVQSRVSKIKGPIL
CLVGPPGVGKTSLGQSIAKATGRQYVRMALGGKLIQKMAKVGVKNPLFLL
DEIDKMAPASALLEVLDPEQNVAFNHYLEVDYDLSDVMFVATSNSMNIPA
PLLDRMEVIRLSGYTEDEKLNIAKQHLLPKQFERNAIKKGELTIDDSAIM
SIIRYYTREAGVRSLEREISKLCRKAVKNLLMDKTVKHIEINGDNLKDFL
GVQKVDYGRADTENRVGQVTGLAWTEVGGDLLTIETACVPGKGKLTYTGS
LGEVMQESIQAALTVVRARADKLGINPDFYEKRDIHVHVPEGATPKDGPS
AGIAMCTALVSCLTGNPVRADVAMTGEITLRGLVLPIGGLKEKLLAAHRG
GIKVVLIPDDNKRDLEEIPDNVIADLEIHPVKRIDDVLAIALEHPA
3D structure
PDB6v11 Structural basis for distinct operational modes and protease activation in AAA+ protease Lon.
ChainB
Resolution3.8 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 B D323 H324 Y325 G359 V360 G361 K362 T363 Y493 R542 D71 H72 Y73 G107 V108 G109 K110 T111 Y214 R263
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:6v11, PDBe:6v11, PDBj:6v11
PDBsum6v11
PubMed32490208
UniProtA0A5P8YJ65

[Back to BioLiP]