Structure of PDB 4naq Chain A

Receptor sequence
>4naqA (length=901) Species: 9823 (Sus scrofa) [Search protein sequence]
SKPWNRYRLPTTLLPDSYNVTLRPYLTPNADGLYIFKGKSIVRFLCQEPT
DVIIIHSKKLNYTTQGHMVVLRGVGDSQVPEIDRTELVELTEYLVVHLKG
SLQPGHMYEMESEFQGELADDLAGFYRSEYMEGNVKKVLATTQMQSTDAR
KSFPCFDEPAMKATFNITLIHPNNLTALSNMPPKGSSTPLAEDPNWSVTE
FETTPVMSTYLLAYIVSEFQSVNETAQNGVLIRIWARPNAIAEGHGMYAL
NVTGPILNFFANHYNTSYPLPKSDQIALPDFNAGAMENWGLVTYRENALL
FDPQSSSISNKERVVTVIAHQLAHQWFGNLVTLAWWNDLWLNEGFASYVE
YLGADHAEPTWNLKDLIVPGDVYRVMAVDALASSHPLTTPAEEVNTPAQI
SEMFDSISYSKGASVIRMLSNFLTEDLFKEGLASYLHAFAYQNTTYLDLW
EHLQKAVDAQTSIRLPDTVRAIMDRWTLQMGFPVITVDTKTGNISQKHFL
LDSESNVTRSSAFDYLWIVPISSIKNGVMQDHYWLRDVSQAQNDLFKTAS
DDWVLLNVNVTGYFQVNYDEDNWRMIQHQLQTNLSVIPVINRAQVIYDSF
NLATAHMVPVTLALDNTLFLNGEKEYMPWQAALSSLSYFSLMFDRSEVYG
PMKKYLRKQVEPLFQHFETLTKNWTERPENLMDQYSEINAISTACSNGLP
QCENLAKTLFDQWMSDPENNPIHPNLRSTIYCNAIAQGGQDQWDFAWGQL
QQAQLVNEADKLRSALACSNEVWLLNRYLGYTLNPDLIRKQDATSTINSI
ASNVIGQPLAWDFVQSNWKKLFQDYGGGSFSFSNLIQGVTRRFSSEFELQ
QLEQFKKNNMDVGFGSGTRALEQALEKTKANIKWVKENKEVVLNWFIEHS
S
3D structure
PDB4naq Structural basis for multifunctional roles of mammalian aminopeptidase N.
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E350 H383 Q384 H387 E406 S464 Y472
Catalytic site (residue number reindexed from 1) E287 H320 Q321 H324 E343 S401 Y409
Enzyme Commision number 3.4.11.2: membrane alanyl 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 A348 M349 E350 H383 Q384 E406 E413 P432 G433 D434 Y472 A285 M286 E287 H320 Q321 E343 E350 P369 G370 D371 Y409
BS02 ZN A H383 H387 E406 H320 H324 E343
Gene Ontology
Molecular Function
GO:0001618 virus receptor activity
GO:0004177 aminopeptidase 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:0006508 proteolysis
GO:0030154 cell differentiation
GO:0043171 peptide catabolic process
GO:0046718 symbiont entry into host cell
Cellular Component
GO:0005615 extracellular space
GO:0005737 cytoplasm
GO:0005886 plasma membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4naq, PDBe:4naq, PDBj:4naq
PDBsum4naq
PubMed23071329
UniProtP15145|AMPN_PIG Aminopeptidase N (Gene Name=ANPEP)

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