Structure of PDB 4fkk Chain A

Receptor sequence
>4fkkA (length=902) Species: 9823 (Sus scrofa) [Search protein sequence]
QSKPWNRYRLPTTLLPDSYNVTLRPYLTPNADGLYIFKGKSIVRFLCQEP
TDVIIIHSKKLNYTTQGHMVVLRGVGDSQVPEIDRTELVELTEYLVVHLK
GSLQPGHMYEMESEFQGELADDLAGFYRSEYMEGNVKKVLATTQMQSTDA
RKSFPCFDEPAMKATFNITLIHPNNLTALSNMPPKGSSTPLAEDPNWSVT
EFETTPVMSTYLLAYIVSEFQSVNETAQNGVLIRIWARPNAIAEGHGMYA
LNVTGPILNFFANHYNTSYPLPKSDQIALPDFNAGAMENWGLVTYRENAL
LFDPQSSSISNKERVVTVIAHELAHQWFGNLVTLAWWNDLWLNEGFASYV
EYLGADHAEPTWNLKDLIVPGDVYRVMAVDALASSHPLTTPAEEVNTPAQ
ISEMFDSISYSKGASVIRMLSNFLTEDLFKEGLASYLHAFAYQNTTYLDL
WEHLQKAVDAQTSIRLPDTVRAIMDRWTLQMGFPVITVDTKTGNISQKHF
LLDSESNVTRSSAFDYLWIVPISSIKNGVMQDHYWLRDVSQAQNDLFKTA
SDDWVLLNVNVTGYFQVNYDEDNWRMIQHQLQTNLSVIPVINRAQVIYDS
FNLATAHMVPVTLALDNTLFLNGEKEYMPWQAALSSLSYFSLMFDRSEVY
GPMKKYLRKQVEPLFQHFETLTKNWTERPENLMDQYSEINAISTACSNGL
PQCENLAKTLFDQWMSDPENNPIHPNLRSTIYCNAIAQGGQDQWDFAWGQ
LQQAQLVNEADKLRSALACSNEVWLLNRYLGYTLNPDLIRKQDATSTINS
IASNVIGQPLAWDFVQSNWKKLFQDYGGGSFSFSNLIQGVTRRFSSEFEL
QQLEQFKKNNMDVGFGSGTRALEQALEKTKANIKWVKENKEVVLNWFIEH
SS
3D structure
PDB4fkk Structural basis for multifunctional roles of mammalian aminopeptidase N.
ChainA
Resolution2.6 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 E384 H387 E406 S464 Y472
Catalytic site (residue number reindexed from 1) E288 H321 E322 H325 E344 S402 Y410
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 BES A A346 A348 M349 E350 H383 E384 H387 E406 Y472 A284 A286 M287 E288 H321 E322 H325 E344 Y410 PDBbind-CN: -logKd/Ki=9.30,Ki=0.5nM
BindingDB: Ki=4100nM,IC50=9400nM
BS02 ZN A H383 H387 E406 H321 H325 E344
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:4fkk, PDBe:4fkk, PDBj:4fkk
PDBsum4fkk
PubMed23071329
UniProtP15145|AMPN_PIG Aminopeptidase N (Gene Name=ANPEP)

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