Structure of PDB 5ly3 Chain A Binding Site BS01

Receptor Information
>5ly3 Chain A (length=427) Species: 181486 (Pyrobaculum calidifontis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ISDAYRLKYTFGVDFGTSYVKYGPITLNEPKMVQTRGLFLRDLPESVKMR
IPPDVLARGLVVGDEEVRKYLSSVRDVQRNLKYPLKDGVARRDDEEAWRV
LKELARYTLAQFPVSDPEFAGWLVAVALSALAPDYMYKAIFDIYDELASE
FKIYAVTILPQPLAVAIAENAVNCVIVEGGHGNIQVAPISFALIREGLVA
LNRGGAEANAITREILKDIGYSDIAREEYAVEVVKRAVGLVPRRLKEAIR
AAKSDPDRFVTKVRLSPVVEVEIPREYAWTRFLIGEIVFDPNHEEIKSYI
EQSRLRIENAVIGDVTLYGEMDVASAIITSLRNVSVEIQERVASQIILSG
GAFSWRVPPGMEDVAADSVTRVKIALEEKSPALASKVEVRLVSEPQYSVW
RGAVIYGYALPLSLEWSDTTREGWRFP
Ligand information
>5ly3 Chain B (length=16) Species: 410359 (Pyrobaculum calidifontis JCM 11548) [Search peptide sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
GGIGENEWVKILRSKR
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB5ly3 Crenactin forms actin-like double helical filaments regulated by arcadin-2.
Resolution1.6 Å
Binding residue
(original residue number in PDB)		A169 I170 N173 A174 V175 F194 Y409 Y411 P414 L417 E425
Binding residue
(residue number reindexed from 1)		A166 I167 N170 A171 V172 F191 Y406 Y408 P411 L414 E422
Enzymatic activity
Enzyme Commision number 3.6.4.-
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016787 hydrolase activity
Cellular Component
GO:0005737 cytoplasm
GO:0005856 cytoskeleton

View graph for
Molecular Function
View graph for
Cellular Component
External links
PDB RCSB:5ly3, PDBe:5ly3, PDBj:5ly3
PDBsum5ly3
PubMed27852434
UniProtA3MWN5|CREN1_PYRCJ Crenactin (Gene Name=cren-1)

[Back to BioLiP]