Structure of PDB 5lhd Chain D

Receptor sequence
>5lhdD (length=904) Species: 9606 (Homo sapiens) [Search protein sequence]
TLDQSKAWNRYRLPNTLKPDSYRVTLRPYLTPNDRGLYVFKGSSTVRFTC
KEATDVIIIHSKKLNYTLSQGHRVVLRGVGGSQPPDIDKTELVEPTEYLV
VHLKGSLVKDSQYEMDSEFEGELADDLAGFYRSEYMEGNVRKVVATTQMQ
AADARKSFPCFDEPAMKAEFNITLIHPKDLTALSNMLPKGPSTPLPEDPN
WNVTEFHTTPKMSTYLLAFIVSEFDYVEKQASNGVLIRIWARPSAIAAGH
GDYALNVTGPILNFFAGHYDTPYPLPKSDQIGLPDFNAGAMENWGLVTYR
ENSLLFDPLSSSSSNKERVVTVIAHELAHQWFGNLVTIEWWNDLWLNEGF
ASYVEYLGADYAEPTWNLKDLMVLNDVYRVMAVDALASSHPLSTPASEIN
TPAQISELFDAISYSKGASVLRMLSSFLSEDVFKQGLASYLHTFAYQNTI
YLNLWDHLQEAVNNRSIQLPTTVRDIMNRWTLQMGFPVITVDTSTGTLSQ
EHFLLDPDSNVTRPSEFNYVWIVPITSIRDGRQQQDYWLIDVRAQNDLFS
TSGNEWVLLNLNVTGYYRVNYDEENWRKIQTQLQRDHSAIPVINRAQIIN
DAFNLASAHKVPVTLALNNTLFLIEERQYMPWEAALSSLSYFKLMFDRSE
VYGPMKNYLKKQVTPLFIHFRNNTNNWREIPENLMDQYSEVNAISTACSN
GVPECEEMVSGLFKQWMENPNNNPIHPNLRSTVYCNAIAQGGEEEWDFAW
EQFRNATLVNEADKLRAALACSKELWILNRYLSYTLNPDLIRKQDATSTI
ISITNNVIGQGLVWDFVQSNWKKLFNDYGGGSFSFSNLIQAVTRRFSTEY
ELQQLEQFKKDNEETGFGSGTRALEQALEKTKANIKWVKENKEVVLQWFT
ENSK
3D structure
PDB5lhd Allosteric inhibition of aminopeptidase N functions related to tumor growth and virus infection.
ChainD
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) E355 H388 E389 H392 E411 S469 Y477
Catalytic site (residue number reindexed from 1) E292 H325 E326 H329 E348 S406 Y414
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 BMA D K172 D173 K109 D110
BS02 ZN D H388 H392 E411 H325 H329 E348
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:5lhd, PDBe:5lhd, PDBj:5lhd
PDBsum5lhd
PubMed28393915
UniProtP15144|AMPN_HUMAN Aminopeptidase N (Gene Name=ANPEP)

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