Structure of PDB 2aj8 Chain A

Receptor sequence
>2aj8A (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
PDB2aj8 Rigidity and flexibility of dipeptidyl peptidase IV: crystal structures of and docking experiments with DPIV.
ChainA
Resolution2.11 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) 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 SC3 A E205 E206 Y547 S630 Y631 V656 Y662 Y666 V711 E167 E168 Y509 S592 Y593 V618 Y624 Y628 V673 MOAD: Ki=638nM
PDBbind-CN: -logKd/Ki=6.20,Ki=638nM
BS02 SC3 A W187 A280 S281 W149 A242 S243 MOAD: Ki=638nM
PDBbind-CN: -logKd/Ki=6.20,Ki=638nM
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2aj8, PDBe:2aj8, PDBj:2aj8
PDBsum2aj8
PubMed16330047
UniProtP22411|DPP4_PIG Dipeptidyl peptidase 4 (Gene Name=DPP4)

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