Structure of PDB 4kx8 Chain A

Receptor sequence
>4kx8A (length=875) Species: 9606 (Homo sapiens) [Search protein sequence]
DICPASEDESGQWKNFRLPDFVNPVHYDLHVKPLLEEDTYTGTVSISINL
SAPTRYLWLHLRETRITRLPELKRPSGDQVQVRRCFEYKKQEYVVVEAEE
ELTPSSGDGLYLLTMEFAGWLNGSLVGFYRTTYTENGRVKSIAATDHEPT
DARKSFPCFDEPNKKATYTISITHPKEYGALSNMPVAKEESVDDKWTRTT
FEKSVPMSTYLVCFAVHQFDSVKRISNSGKPLTIYVQPEQKHTAEYAANI
TKSVFDYFEEYFAMNYSLPKLDKIAIPDFGTGAMENWGLITYRETNLLYD
PKESASSNQQRVATVVAHELVHQWFGNIVTMDWWEDLWLNEGFASFFEFL
GVNHAETDWQMRDQMLLEDVLPVQEDDSLMSSHPIIVTVTTPDEITSVFD
GISYSKGSSILRMLEDWIKPENFQKGCQMYLEKYQFKNAKTSDFWAALEE
ASRLPVKEVMDTWTRQMGYPVLNVNGVKNITQKRFLLDPRANPSQPPSDL
GYTWNIPVKWTEDNITSSVLFNRSEKEGITLNSGNAFLKINPDHIGFYRV
NYEVATWDSIATALSLNHKTFSSADRASLIDDAFALARAQLLDYKVALNL
TKYLKREENFLPWQRVISAVTYIISMFEDDKELYPMIEEYFQGQVKPIAD
SLGWNDAGDHVTKLLRSSVLGFACKMGDREALNNASSLFEQWLNGTVSLP
VNLRLLVYRYGMQNSGNEISWNYTLEQYQKTSLAQEKEKLLYGLASVKNV
TLLSRYLDLLKDTNLIKTQDVFTVIRYISYNSYGKNMAWNWIQLNWDYLV
NRYTLNNRNLGRIVTIAEPFNTELQLWQMESFFAKYPQAGAGEKPREQVL
ETVKNNIEWLKQHRNTIREWFFNLL
3D structure
PDB4kx8 Structural insights into central hypertension regulation by human aminopeptidase a.
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E360 H393 E394 H397 E416 T471 Y479
Catalytic site (residue number reindexed from 1) E285 H318 E319 H322 E341 T396 Y404
Enzyme Commision number 3.4.11.7: glutamyl aminopeptidase.
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 peptide A E223 T356 G357 A358 E360 N371 R386 H393 E394 E416 Y479 R887 E148 T281 G282 A283 E285 N296 R311 H318 E319 E341 Y404 R808
BS02 ZN A H393 H397 E416 H318 H322 E341
Gene Ontology
Molecular Function
GO:0004177 aminopeptidase activity
GO:0008233 peptidase activity
GO:0008237 metallopeptidase activity
GO:0008270 zinc ion binding
GO:0042277 peptide binding
GO:0046872 metal ion binding
GO:0070006 metalloaminopeptidase activity
Biological Process
GO:0001525 angiogenesis
GO:0002003 angiotensin maturation
GO:0003081 regulation of systemic arterial blood pressure by renin-angiotensin
GO:0006508 proteolysis
GO:0007267 cell-cell signaling
GO:0008217 regulation of blood pressure
GO:0008283 cell population proliferation
GO:0016477 cell migration
GO:0032835 glomerulus development
GO:0043171 peptide catabolic process
Cellular Component
GO:0005615 extracellular space
GO:0005737 cytoplasm
GO:0005765 lysosomal membrane
GO:0005886 plasma membrane
GO:0005903 brush border
GO:0009897 external side of plasma membrane
GO:0016324 apical plasma membrane
GO:0031410 cytoplasmic vesicle
GO:0045177 apical part of cell
GO:0070062 extracellular exosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4kx8, PDBe:4kx8, PDBj:4kx8
PDBsum4kx8
PubMed23888046
UniProtQ07075|AMPE_HUMAN Glutamyl aminopeptidase (Gene Name=ENPEP)

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