Structure of PDB 4n8d Chain A

Receptor sequence
>4n8dA (length=727) Species: 9606 (Homo sapiens) [Search protein sequence]
RKTYTLTDYLKNTYRLKLYSLRWISDHEYLYKQENNILVFNAEYGNSSVF
LENSTFDEFGHSINDYSISPDGQFILLEYNYVKQWRHSYTASYDIYDLNK
RQLITEERIPNNTQWVTWSPVGHKLAYVWNNDIYVKIEPNLPSYRITWTG
KEDIIYNGITDWVYEEEVFSAYSALWWSPNGTFLAYAQFNDTEVPLIEYS
FYSDESLQYPKTVRVPYPKAGAVNPTVKFFVVNTDSLSSVTNATSIQITA
PASMLIGDHYLCDVTWATQERISLQWLRRIQNYSVMDICDYDESSGRWNC
LVARQHIEMSTTGWVGRFRPSEPHFTLDGNSFYKIISNEEGYRHICYFQI
DKKDCTFITKGTWEVIGIEALTSDYLYYISNEYKGMPGGRNLYKIQLIDY
TKVTCLSCELNPERCQYYSVSFSKEAKYYQLRCSGPGLPLYTLHSSVNDK
GLRVLEDNSALDKMLQNVQMPSKKLDFIILNETKFWYQMILPPHFDKSKK
YPLLLDVYAGPCSQKADTVFRLNWATYLASTENIIVASFDGRGSGYQGDK
IMHAINRRLGTFEVEDQIEAARQFSKMGFVDNKRIAIWGWSYGGYVTSMV
LGSGSGVFKCGIAVAPVSRWEYYDSVYTERYMGLPTPEDNLDHYRNSTVM
SRAENFKQVEYLLIHGTADDNVHFQQSAQISKALVDVGVDFQAMWYTDED
HGIASSTAHQHIYTHMSHFIKQCFSLP
3D structure
PDB4n8d Discovery of C-(1-aryl-cyclohexyl)-methylamines as selective, orally available inhibitors of dipeptidyl peptidase IV.
ChainA
Resolution1.65 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y547 S630 Y631 D708 H740
Catalytic site (residue number reindexed from 1) Y508 S591 Y592 D669 H701
Enzyme Commision number 3.4.14.5: dipeptidyl-peptidase IV.
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 2KS A E205 E206 R358 Y662 Y666 V711 E166 E167 R319 Y623 Y627 V672 MOAD: ic50=11.9uM
PDBbind-CN: -logKd/Ki=4.92,IC50=11.9uM
Gene Ontology
Molecular Function
GO:0001618 virus receptor activity
GO:0002020 protease binding
GO:0004177 aminopeptidase activity
GO:0004252 serine-type endopeptidase activity
GO:0005102 signaling receptor binding
GO:0005515 protein binding
GO:0008236 serine-type peptidase activity
GO:0008239 dipeptidyl-peptidase activity
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
GO:0045499 chemorepellent activity
Biological Process
GO:0001662 behavioral fear response
GO:0001666 response to hypoxia
GO:0006508 proteolysis
GO:0007155 cell adhesion
GO:0008284 positive regulation of cell population proliferation
GO:0010716 negative regulation of extracellular matrix disassembly
GO:0016486 peptide hormone processing
GO:0019065 receptor-mediated endocytosis of virus by host cell
GO:0031295 T cell costimulation
GO:0033632 regulation of cell-cell adhesion mediated by integrin
GO:0035641 locomotory exploration behavior
GO:0036343 psychomotor behavior
GO:0042110 T cell activation
GO:0043542 endothelial cell migration
GO:0046718 symbiont entry into host cell
GO:0046813 receptor-mediated virion attachment to host cell
GO:0050919 negative chemotaxis
GO:0061025 membrane fusion
GO:0090024 negative regulation of neutrophil chemotaxis
GO:0120116 glucagon processing
Cellular Component
GO:0005576 extracellular region
GO:0005765 lysosomal membrane
GO:0005886 plasma membrane
GO:0005925 focal adhesion
GO:0009986 cell surface
GO:0016020 membrane
GO:0016324 apical plasma membrane
GO:0030027 lamellipodium
GO:0030139 endocytic vesicle
GO:0031258 lamellipodium membrane
GO:0042995 cell projection
GO:0045121 membrane raft
GO:0046581 intercellular canaliculus
GO:0070062 extracellular exosome
GO:0070161 anchoring junction

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4n8d, PDBe:4n8d, PDBj:4n8d
PDBsum4n8d
PubMed24439847
UniProtP27487|DPP4_HUMAN Dipeptidyl peptidase 4 (Gene Name=DPP4)

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