Structure of PDB 3g0g Chain D

Receptor sequence
>3g0gD (length=690) Species: 9606 (Homo sapiens) [Search protein sequence]
KTYTLTDYLKNTYRLKLYSLRWISDHEYLYSINDYSISPDGQFILLEYNY
VKQWRHSYTASYDIYDITEERIPNNTQWVTWSPVGHKLAYVWNNDIYVKI
EPNLPSYRITWTGKEDIIYNGITDWVYEEEVFSAYSALWWSPNGTFLAYA
QFNDTEVPLIEYSFYSDESLQYPKTVRVPYPKAGAVNPTVKFFVVNTDSL
SSVTNATSIQITAPASMLIGDHYLCDVTWATQERISLQWLRRIQNYSVMD
ICDYDESSGRWNCLVARQHIEMSTTGWVGRFRPSEPHFTLDGNSFYKIIS
NEEGYRHICYFQIDKKDCTFITKGTWEVIGIEALTSDYLYYISNEYKGMP
GGRNLYKIQLSDYTKVTCLSCELNPERCQYYSVSFSKEAKYYQLRCSGPG
LPLYTLHSSVNDKGLRVLEDNSALDKMLQNVQMPSKKLDFIILNETKFWY
QMILPPHFDKSKKYPLLLDVYAGPCSQKADTVFRLNWATYLASTENIIVA
SFDGRGSGYQGDKIMHAINRRLGTFEVEDQIEAARQFSKMGFVDNKRIAI
WGWSYGGYVTSMVLGSGSGVFKCGIAVAPVSRWEYYDSVYTERYMGLPTP
EDNLDHYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQSAQISKALVDV
GVDFQAMWYTDEDHGIASSTAHQHIYTHMSHFIKQCFSLP
3D structure
PDB3g0g Design and Synthesis of Pyrimidinone and Pyrimidinedione Inhibitors of Dipeptidyl Peptidase IV.
ChainD
Resolution2.45 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) Y547 S630 Y631 D708 H740
Catalytic site (residue number reindexed from 1) Y471 S554 Y555 D632 H664
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 RUM D R125 E205 E206 Y547 S630 Y631 Y662 Y666 V711 R55 E129 E130 Y471 S554 Y555 Y586 Y590 V635 MOAD: ic50=0.005uM
BindingDB: IC50=5nM
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:3g0g, PDBe:3g0g, PDBj:3g0g
PDBsum3g0g
PubMed21186796
UniProtP27487|DPP4_HUMAN Dipeptidyl peptidase 4 (Gene Name=DPP4)

[Back to BioLiP]