Structure of PDB 4re6 Chain A

Receptor sequence
>4re6A (length=577) Species: 272557 (Aeropyrum pernix K1) [Search protein sequence]
MPVEFSRIVRDVERLIAVEKYSLQGVVDGDKLLVVGFSEGSVNAYLYDGG
ETVKLNREPINSVLDPHYGVGRVILVRDVSKGAEQHALFKVNTSRPGEEQ
RLEAVKPMRILSGVDTGEAVVFTGATEDRVALYALDGGGLRELARLPGFG
FVSDIRGDLIAGLGFFGGGRVSLFTSNLSSGGLRVFDSGEGSFSSASISP
GMKVTAGLETAREARLVTVDPRDGSVEDLELPSKDFSSYRPTAITWLGYL
PDGRLAVVARREGRSAVFIDGERVEAPQGNHGRVVLWRGKLVTSHTSLST
PPRIVSLPSGEPLLEGGLPEDLRRSIAGSRLVWVESFDGSRVPTYVLESG
RAPTPGPTVVLVHGGPFAEDSDSWDTFAASLAAAGFHVVMPNYRGSTGYG
EEWRLKIIGDPCGGELEDVSAAARWARESGLASELYIMGYSYGGYMTLCA
LTMKPGLFKAGVAGASVVDWEEMYELSDAAFRNFIEQLTGGSREIMRSRS
PINHVDRIKEPLALIHPQNDSRTPLKPLLRLMGELLARGKTFEAHIIPDA
GHAINTMEDAVKILLPAVFFLATQRER
3D structure
PDB4re6 Catalytically distinct states captured in a crystal lattice: the substrate-bound and scavenger states of acylaminoacyl peptidase and their implications for functionality.
ChainA
Resolution2.55 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S42 E43
Catalytic site (residue number reindexed from 1) S38 E39
Enzyme Commision number 3.4.19.1: acylaminoacyl-peptidase.
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 Y3A A G369 S445 M477 F485 F488 R526 H556 G365 S441 M473 F481 F484 R522 H552
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
GO:0008236 serine-type peptidase activity
GO:0008242 omega peptidase activity
GO:0016787 hydrolase activity
Biological Process
GO:0006508 proteolysis
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4re6, PDBe:4re6, PDBj:4re6
PDBsum4re6
PubMed25760596
UniProtQ9YBQ2|APEH_AERPE Acylamino-acid-releasing enzyme (Gene Name=APE_1547.1)

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