Structure of PDB 3vjl Chain B

Receptor sequence
>3vjlB (length=729) Species: 9606 (Homo sapiens) [Search protein sequence]
DSRKTYTLTDYLKNTYRLKLYSLRWISDHEYLYKQENNILVFNAEYGNSS
VFLENSTFDEFGHSINDYSISPDGQFILLEYNYVKQWRHSYTASYDIYDL
NKRQLITEERIPNNTQWVTWSPVGHKLAYVWNNDIYVKIEPNLPSYRITW
TGKEDIIYNGITDWVYEEEVFSAYSALWWSPNGTFLAYAQFNDTEVPLIE
YSFYSDESLQYPKTVRVPYPKAGAVNPTVKFFVVNTDSLSSVTNATSIQI
TAPASMLIGDHYLCDVTWATQERISLQWLRRIQNYSVMDICDYDESSGRW
NCLVARQHIEMSTTGWVGRFRPSEPHFTLDGNSFYKIISNEEGYRHICYF
QIDKKDCTFITKGTWEVIGIEALTSDYLYYISNEYKGMPGGRNLYKIQLS
DYTKVTCLSCELNPERCQYYSVSFSKEAKYYQLRCSGPGLPLYTLHSSVN
DKGLRVLEDNSALDKMLQNVQMPSKKLDFIILNETKFWYQMILPPHFDKS
KKYPLLLDVYAGPCSQKADTVFRLNWATYLASTENIIVASFDGRGSGYQG
DKIMHAINRRLGTFEVEDQIEAARQFSKMGFVDNKRIAIWGWSYGGYVTS
MVLGSGSGVFKCGIAVAPVSRWEYYDSVYTERYMGLPTPEDNLDHYRNST
VMSRAENFKQVEYLLIHGTADDNVHFQQSAQISKALVDVGVDFQAMWYTD
EDHGIASSTAHQHIYTHMSHFIKQCFSLP
3D structure
PDB3vjl Discovery and preclinical profile of teneligliptin (3-[(2S,4S)-4-[4-(3-methyl-1-phenyl-1H-pyrazol-5-yl)piperazin-1-yl]pyrrolidin-2-ylcarbonyl]thiazolidine): A highly potent, selective, long-lasting and orally active dipeptidyl peptidase IV inhibitor for the treatment of type 2 diabetes
ChainB
Resolution2.393 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) Y510 S593 Y594 D671 H703
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 W94 B E205 E206 F357 S630 Y631 Y662 Y666 N710 E168 E169 F320 S593 Y594 Y625 Y629 N673 MOAD: ic50=5.6nM
BindingDB: IC50=5.6nM
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

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Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3vjl, PDBe:3vjl, PDBj:3vjl
PDBsum3vjl
PubMed22959556
UniProtP27487|DPP4_HUMAN Dipeptidyl peptidase 4 (Gene Name=DPP4)

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