Structure of PDB 6atk Chain C

Receptor sequence
>6atkC (length=891) Species: 9606 (Homo sapiens) [Search protein sequence]
SKAWNRYRLPNTLKPDSYRVTLRPYLTPNDRGLYVFKGSSTVRFTCKEAT
DVIIIHSKKLNYTLSQGHRVVLRGVGGSQPPDIDKTELVEPTEYLVVHLK
GSLVKDSQYEMDSEFEGELADDLAGFYRSEYMEGNVRKVVATTQMQAADA
RKSFPCFDEPAMKAEFNITLIHPKDLTALSNMLPKGPSTPLPEDPNWNVT
EFHTTPKMSTYLLAFIVSEFDYVEKQASNGVLIRIWARPSAIAAGHGDYA
LNVTGPILNFFAGHYDTPYPLPKSDQIGLPDFNAGAMENWGLVTYRENSL
LFDPLSSSSSNKERVVTVIAHELAHQWFGNLVTIEWWNDLWLNEGFASYV
EYLGADYAEPTWNLKDLMVLNDVYRVMAVDALASSHPLSTPASEINTPAQ
ISELFDAISYSKGASVLRMLSSFLSEDVFKQGLASYLHTFAYQNTIYLNL
WDHLQEAVNNRSIQLPTTVRDIMNRWTLQMGFPVITVDTSTGTLSQEHFL
LDPDSNVTRPSEFNYVWIVPITSIRDGRQQQDYWLIDVRAQNDLFSTSGN
EWVLLNLNVTGYYRVNYDEENWRKIQTQLQRDHSAIPVINRAQIINDAFN
LASAHKVPVTLALNNTLFLIEERQYMPWEAALSSLSYFKLMFDRSEVYGP
MKNYLKKQVTPLFIHFRNNTNNWREIPENLMDQYSEVNAISTACSNGVPE
CEEMVSGLFKQWMENPNNNPIHPNLRSTVYCNAIAQGGEEEWDFAWEQFR
NATLVNEADKLRAALACSKELWILNRYLSYTLNPDLIRKQDATSTIISIT
NNVIGQGLVWDFVQSNWKKLFNSNLIQAVTRRFSTEYELQQLEQFKKDNE
ETGFGSGTRALEQALEKTKANIKWVKENKEVVLQWFTENSK
3D structure
PDB6atk Receptor-binding loops in alphacoronavirus adaptation and evolution.
ChainC
Resolution3.505 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) 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 peptide C T244 E286 D288 Y289 V290 E291 T177 E219 D221 Y222 V223 E224
BS02 ZN C H388 H392 E411 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: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:6atk, PDBe:6atk, PDBj:6atk
PDBsum6atk
PubMed29170370
UniProtP15144|AMPN_HUMAN Aminopeptidase N (Gene Name=ANPEP)

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