Structure of PDB 2i3z Chain A

Receptor sequence
>2i3zA (length=730) Species: 10116 (Rattus norvegicus) [Search protein sequence]
RRTYTLADYLKNTFRVKSYSLRWVSDSEYLYKQENNILLFNAEHGNSSIF
LENSTFEIFGDSISDYSVSPDRLFVLLEYNYVKQWRHSYTASYSIYDLNK
RQLITEEKIPNNTQWITWSQEGHKLAYVWKNDIYVKIEPHLPSHRITSTG
KENVIFNGINDWVYEEEIFGAYSALWWSPNGTFLAYAQFNDTGVPLIEYS
FYSDESLQYPKTVWIPYPKAGAVNPTVKFFIVNTDSLSSTTTTIPMQITA
PASVTTGDHYLCDVAWVSEDRISLQWLRRIQNYSVMAICDYDKTTLVWNC
PTTQEHIETSATGWCGRFRPAEPHFTSDGSSFYKIVSDKDGYKHICQFQK
DRKPEQVCTFITKGAWEVISIEALTSDYLYYISNEYKEMPGGRNLYKIQL
TDHTNKKCLSCDLNPERCQYYSVSLSKEAKYYQLGCRGPGLPLYTLHRST
DQKELRVLEDNSALDKMLQDVQMPSKKLDFIVLNETRFWYQMILPPHFDK
SKKYPLLIDVYAGPCSQKADAAFRLNWATYLASTENIIVASFDGRGSGYQ
GDKIMHAINKRLGTLEVEDQIEAARQFLKMGFVDSKRVAIWGWSYGGYVT
SMVLGSGSGVFKCGIAVAPVSRWEYYDSVYTERYMGLPTPEDNLDHYRNS
TVMSRAENFKQVEYLLIHGTADDNVHFQQSAQISKALVDAGVDFQAMWYT
DEDHGIASSTAHQHIYSHMSHFLQQCFSLR
3D structure
PDB2i3z Xanthine mimetics as potent dipeptidyl peptidase IV inhibitors.
ChainA
Resolution2.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y548 S631 Y632 D709 H741
Catalytic site (residue number reindexed from 1) Y511 S594 Y595 D672 H704
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 LIR A E203 E204 F355 Y548 S631 Y632 Y663 Y667 E166 E167 F318 Y511 S594 Y595 Y626 Y630 PDBbind-CN: -logKd/Ki=8.70,Ki=2nM
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:0005518 collagen binding
GO:0008236 serine-type peptidase activity
GO:0008239 dipeptidyl-peptidase activity
GO:0042277 peptide binding
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:0002337 B-1a B cell differentiation
GO:0002709 regulation of T cell mediated immunity
GO:0002717 positive regulation of natural killer cell mediated immunity
GO:0006508 proteolysis
GO:0007155 cell adhesion
GO:0008284 positive regulation of cell population proliferation
GO:0010716 negative regulation of extracellular matrix disassembly
GO:0030163 protein catabolic process
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:0050919 negative chemotaxis
GO:0090024 negative regulation of neutrophil chemotaxis
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:0046581 intercellular canaliculus
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:2i3z, PDBe:2i3z, PDBj:2i3z
PDBsum2i3z
PubMed17010607
UniProtP14740|DPP4_RAT Dipeptidyl peptidase 4 (Gene Name=Dpp4)

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