Structure of PDB 2hu7 Chain B

Receptor sequence
>2hu7B (length=573) Species: 56636 (Aeropyrum pernix) [Search protein sequence]
FSRIVRDVERLIAVEKYSLQGVVDGDKLLVVGFSEGSVNAYLYDGGETVK
LNREPINSVLDPHYGVGRVILVRDVSKGAEQHALFKVNTSRPGEEQRLEA
VKPMRILSGVDTGEAVVFTGATEDRVALYALDGGGLRELARLPGFGFVSD
IRGDLIAGLGFFGGGRVSLFTSNLSSGGLRVFDSGEGSFSSASISPGMKV
TAGLETAREARLVTVDPRDGSVEDLELPSKDFSSYRPTAITWLGYLPDGR
LAVVARREGRSAVFIDGERVEAPQGNHGRVVLWRGKLVTSHTSLSTPPRI
VSLPSGEPLLEGGLPEDLRRSIAGSRLVWVESFDGSRVPTYVLESGRAPT
PGPTVVLVHGGPFAEDSDSWDTFAASLAAAGFHVVMPNYRGSTGYGEEWR
LKIIGDPCGGELEDVSAAARWARESGLASELYIMGYSYGGYMTLCALTMK
PGLFKAGVAGASVVDWEEMYELSDAAFRNFIEQLTGGSREIMRSRSPINH
VDRIKEPLALIHPQNDSRTPLKPLLRLMGELLARGKTFEAHIIPDAGHAI
NTMEDAVKILLPAVFFLATQRER
3D structure
PDB2hu7 The Acylaminoacyl Peptidase from Aeropyrum pernix K1 Thought to Be an Exopeptidase Displays Endopeptidase Activity
ChainB
Resolution2.01 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) S34 E35
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 PHE B G368 G369 S445 Y446 F485 F488 G360 G361 S437 Y438 F477 F480
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:2hu7, PDBe:2hu7, PDBj:2hu7
PDBsum2hu7
PubMed17350041
UniProtQ9YBQ2|APEH_AERPE Acylamino-acid-releasing enzyme (Gene Name=APE_1547.1)

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