Structure of PDB 2bua Chain B

Receptor sequence
>2buaB (length=728) Species: 9823 (Sus scrofa) [Search protein sequence]
SRRTYTLTDYLKSTFRVKFYTLQWISDHEYLYKQENNILLFNAEYGNSSI
FLENSTFDELGYSTNDYSVSPDRQFILFEYNYVKQWRHSYTASYDIYDLN
KRQLITEERIPNNTQWITWSPVGHKLAYVWNNDIYVKNEPNLSSQRITWT
GKENVIYNGVTDWVYEEEVFSAYSALWWSPNGTFLAYAQFNDTEVPLIEY
SFYSDESLQYPKTVRIPYPKAGAENPTVKFFVVDTRTLSPNASVTSYQIV
PPASVLIGDHYLCGVTWVTEERISLQWIRRAQNYSIIDICDYDESTGRWI
SSVARQHIEISTTGWVGRFRPAEPHFTSDGNSFYKIISNEEGYKHICHFQ
TDKSNCTFITKGAWEVIGIEALTSDYLYYISNEHKGMPGGRNLYRIQLND
YTKVTCLSCELNPERCQYYSASFSNKAKYYQLRCFGPGLPLYTLHSSSSD
KELRVLEDNSALDKMLQDVQMPSKKLDVINLHGTKFWYQMILPPHFDKSK
KYPLLIEVYAGPCSQKVDTVFRLSWATYLASTENIIVASFDGRGSGYQGD
KIMHAINRRLGTFEVEDQIEATRQFSKMGFVDDKRIAIWGWSYGGYVTSM
VLGAGSGVFKCGIAVAPVSKWEYYDSVYTERYMGLPTPEDNLDYYRNSTV
MSRAENFKQVEYLLIHGTADDNVHFQQSAQLSKALVDAGVDFQTMWYTDE
DHGIASNMAHQHIYTHMSHFLKQCFSLP
3D structure
PDB2bua The reversed binding of beta-phenethylamine inhibitors of DPP-IV: X-ray structures and properties of novel fragment and elaborated inhibitors.
ChainB
Resolution2.56 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) Y509 S592 Y593 D670 H702
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 007 B E205 E206 Y547 Y662 Y666 V711 E167 E168 Y509 Y624 Y628 V673 BindingDB: IC50=30000nM
Gene Ontology
Molecular Function
GO:0002020 protease binding
GO:0004177 aminopeptidase activity
GO:0004252 serine-type endopeptidase activity
GO:0005102 signaling receptor binding
GO:0008236 serine-type peptidase activity
GO:0008239 dipeptidyl-peptidase activity
GO:0042803 protein homodimerization activity
Biological Process
GO:0006508 proteolysis
GO:0007155 cell adhesion
GO:0008284 positive regulation of cell population proliferation
GO:0010716 negative regulation of extracellular matrix disassembly
GO:0031295 T cell costimulation
GO:0043542 endothelial cell migration
Cellular Component
GO:0005576 extracellular region
GO:0005886 plasma membrane
GO:0009986 cell surface
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:0070161 anchoring junction

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:2bua, PDBe:2bua, PDBj:2bua
PDBsum2bua
PubMed16376544
UniProtP22411|DPP4_PIG Dipeptidyl peptidase 4 (Gene Name=DPP4)

[Back to BioLiP]