Structure of PDB 4fyt Chain A

Receptor sequence
>4fytA (length=903) Species: 9606 (Homo sapiens) [Search protein sequence]
PDQSKAWNRYRLPNTLKPDSYRVTLRPYLTPNDRGLYVFKGSSTVRFTCK
EATDVIIIHSKKLNYTLSQGHRVVLRGVGGSQPPDIDKTELVEPTEYLVV
HLKGSLVKDSQYEMDSEFEGELADDLAGFYRSEYMEGNVRKVVATTQMQA
ADARKSFPCFDEPAMKAEFNITLIHPKDLTALSNMLPKGPSTPLPEDPNW
NVTEFHTTPKMSTYLLAFIVSEFDYVEKQASNGVLIRIWARPSAIAAGHG
DYALNVTGPILNFFAGHYDTPYPLPKSDQIGLPDFNAGAMENWGLVTYRE
NSLLFDPLSSSSSNKERVVTVIAHELAHQWFGNLVTIEWWNDLWLNEGFA
SYVEYLGADYAEPTWNLKDLMVLNDVYRVMAVDALASSHPLSTPASEINT
PAQISELFDAISYSKGASVLRMLSSFLSEDVFKQGLASYLHTFAYQNTIY
LNLWDHLQEAVNNRSIQLPTTVRDIMNRWTLQMGFPVITVDTSTGTLSQE
HFLLDPDSNVTRPSEFNYVWIVPITSIRDGRQQQDYWLIDVRAQNDLFST
SGNEWVLLNLNVTGYYRVNYDEENWRKIQTQLQRDHSAIPVINRAQIIND
AFNLASAHKVPVTLALNNTLFLIEERQYMPWEAALSSLSYFKLMFDRSEV
YGPMKNYLKKQVTPLFIHFRNNTNNWREIPENLMDQYSEVNAISTACSNG
VPECEEMVSGLFKQWMENPNNNPIHPNLRSTVYCNAIAQGGEEEWDFAWE
QFRNATLVNEADKLRAALACSKELWILNRYLSYTLNPDLIRKQDATSTII
SITNNVIGQGLVWDFVQSNWKKLFNDYGGGSFSFSNLIQAVTRRFSTEYE
LQQLEQFKKDNEETGFGSGTRALEQALEKTKANIKWVKENKEVVLQWFTE
NSK
3D structure
PDB4fyt The X-ray Crystal Structure of Human Aminopeptidase N Reveals a Novel Dimer and the Basis for Peptide Processing.
ChainA
Resolution1.85 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E355 H388 E389 H392 E411 S469 Y477
Catalytic site (residue number reindexed from 1) E291 H324 E325 H328 E347 S405 Y413
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 Q213 A351 G352 A353 M354 E355 R363 R381 H388 E389 H392 E411 Y477 F896 Q149 A287 G288 A289 M290 E291 R299 R317 H324 E325 H328 E347 Y413 F832
BS02 ZN A H388 H392 E411 H324 H328 E347
Gene Ontology
Molecular Function
GO:0001618 virus receptor activity
GO:0004177 aminopeptidase activity
GO:0008237 metallopeptidase activity
GO:0008270 zinc ion binding
GO:0038023 signaling receptor activity
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:0005765 lysosomal membrane
GO:0005793 endoplasmic reticulum-Golgi intermediate compartment
GO:0005886 plasma membrane
GO:0009897 external side of plasma membrane
GO:0030667 secretory granule membrane
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:4fyt, PDBe:4fyt, PDBj:4fyt
PDBsum4fyt
PubMed22932899
UniProtP15144|AMPN_HUMAN Aminopeptidase N (Gene Name=ANPEP)

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