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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

5Y7K

Crystal structure of human DPP4 in complex with inhibitor1

Functional Information from GO Data
ChainGOidnamespacecontents
A0001618molecular_functionvirus receptor activity
A0001662biological_processbehavioral fear response
A0001666biological_processresponse to hypoxia
A0002020molecular_functionprotease binding
A0004177molecular_functionaminopeptidase activity
A0004252molecular_functionserine-type endopeptidase activity
A0005102molecular_functionsignaling receptor binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005765cellular_componentlysosomal membrane
A0005886cellular_componentplasma membrane
A0005925cellular_componentfocal adhesion
A0006508biological_processproteolysis
A0007155biological_processcell adhesion
A0008233molecular_functionpeptidase activity
A0008236molecular_functionserine-type peptidase activity
A0008239molecular_functiondipeptidyl-peptidase activity
A0008284biological_processpositive regulation of cell population proliferation
A0009986cellular_componentcell surface
A0010716biological_processnegative regulation of extracellular matrix disassembly
A0016020cellular_componentmembrane
A0016324cellular_componentapical plasma membrane
A0016486biological_processpeptide hormone processing
A0016787molecular_functionhydrolase activity
A0019065biological_processreceptor-mediated endocytosis of virus by host cell
A0030027cellular_componentlamellipodium
A0030139cellular_componentendocytic vesicle
A0031258cellular_componentlamellipodium membrane
A0031295biological_processT cell costimulation
A0033632biological_processregulation of cell-cell adhesion mediated by integrin
A0035641biological_processlocomotory exploration behavior
A0036343biological_processpsychomotor behavior
A0042110biological_processT cell activation
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0042995cellular_componentcell projection
A0043542biological_processendothelial cell migration
A0045121cellular_componentmembrane raft
A0045499molecular_functionchemorepellent activity
A0046581cellular_componentintercellular canaliculus
A0046718biological_processsymbiont entry into host cell
A0046813biological_processreceptor-mediated virion attachment to host cell
A0050919biological_processnegative chemotaxis
A0061025biological_processmembrane fusion
A0070062cellular_componentextracellular exosome
A0070161cellular_componentanchoring junction
A0090024biological_processnegative regulation of neutrophil chemotaxis
A0120116biological_processglucagon processing
B0001618molecular_functionvirus receptor activity
B0001662biological_processbehavioral fear response
B0001666biological_processresponse to hypoxia
B0002020molecular_functionprotease binding
B0004177molecular_functionaminopeptidase activity
B0004252molecular_functionserine-type endopeptidase activity
B0005102molecular_functionsignaling receptor binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005765cellular_componentlysosomal membrane
B0005886cellular_componentplasma membrane
B0005925cellular_componentfocal adhesion
B0006508biological_processproteolysis
B0007155biological_processcell adhesion
B0008233molecular_functionpeptidase activity
B0008236molecular_functionserine-type peptidase activity
B0008239molecular_functiondipeptidyl-peptidase activity
B0008284biological_processpositive regulation of cell population proliferation
B0009986cellular_componentcell surface
B0010716biological_processnegative regulation of extracellular matrix disassembly
B0016020cellular_componentmembrane
B0016324cellular_componentapical plasma membrane
B0016486biological_processpeptide hormone processing
B0016787molecular_functionhydrolase activity
B0019065biological_processreceptor-mediated endocytosis of virus by host cell
B0030027cellular_componentlamellipodium
B0030139cellular_componentendocytic vesicle
B0031258cellular_componentlamellipodium membrane
B0031295biological_processT cell costimulation
B0033632biological_processregulation of cell-cell adhesion mediated by integrin
B0035641biological_processlocomotory exploration behavior
B0036343biological_processpsychomotor behavior
B0042110biological_processT cell activation
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0042995cellular_componentcell projection
B0043542biological_processendothelial cell migration
B0045121cellular_componentmembrane raft
B0045499molecular_functionchemorepellent activity
B0046581cellular_componentintercellular canaliculus
B0046718biological_processsymbiont entry into host cell
B0046813biological_processreceptor-mediated virion attachment to host cell
B0050919biological_processnegative chemotaxis
B0061025biological_processmembrane fusion
B0070062cellular_componentextracellular exosome
B0070161cellular_componentanchoring junction
B0090024biological_processnegative regulation of neutrophil chemotaxis
B0120116biological_processglucagon processing
C0001618molecular_functionvirus receptor activity
C0001662biological_processbehavioral fear response
C0001666biological_processresponse to hypoxia
C0002020molecular_functionprotease binding
C0004177molecular_functionaminopeptidase activity
C0004252molecular_functionserine-type endopeptidase activity
C0005102molecular_functionsignaling receptor binding
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005765cellular_componentlysosomal membrane
C0005886cellular_componentplasma membrane
C0005925cellular_componentfocal adhesion
C0006508biological_processproteolysis
C0007155biological_processcell adhesion
C0008233molecular_functionpeptidase activity
C0008236molecular_functionserine-type peptidase activity
C0008239molecular_functiondipeptidyl-peptidase activity
C0008284biological_processpositive regulation of cell population proliferation
C0009986cellular_componentcell surface
C0010716biological_processnegative regulation of extracellular matrix disassembly
C0016020cellular_componentmembrane
C0016324cellular_componentapical plasma membrane
C0016486biological_processpeptide hormone processing
C0016787molecular_functionhydrolase activity
C0019065biological_processreceptor-mediated endocytosis of virus by host cell
C0030027cellular_componentlamellipodium
C0030139cellular_componentendocytic vesicle
C0031258cellular_componentlamellipodium membrane
C0031295biological_processT cell costimulation
C0033632biological_processregulation of cell-cell adhesion mediated by integrin
C0035641biological_processlocomotory exploration behavior
C0036343biological_processpsychomotor behavior
C0042110biological_processT cell activation
C0042802molecular_functionidentical protein binding
C0042803molecular_functionprotein homodimerization activity
C0042995cellular_componentcell projection
C0043542biological_processendothelial cell migration
C0045121cellular_componentmembrane raft
C0045499molecular_functionchemorepellent activity
C0046581cellular_componentintercellular canaliculus
C0046718biological_processsymbiont entry into host cell
C0046813biological_processreceptor-mediated virion attachment to host cell
C0050919biological_processnegative chemotaxis
C0061025biological_processmembrane fusion
C0070062cellular_componentextracellular exosome
C0070161cellular_componentanchoring junction
C0090024biological_processnegative regulation of neutrophil chemotaxis
C0120116biological_processglucagon processing
D0001618molecular_functionvirus receptor activity
D0001662biological_processbehavioral fear response
D0001666biological_processresponse to hypoxia
D0002020molecular_functionprotease binding
D0004177molecular_functionaminopeptidase activity
D0004252molecular_functionserine-type endopeptidase activity
D0005102molecular_functionsignaling receptor binding
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005765cellular_componentlysosomal membrane
D0005886cellular_componentplasma membrane
D0005925cellular_componentfocal adhesion
D0006508biological_processproteolysis
D0007155biological_processcell adhesion
D0008233molecular_functionpeptidase activity
D0008236molecular_functionserine-type peptidase activity
D0008239molecular_functiondipeptidyl-peptidase activity
D0008284biological_processpositive regulation of cell population proliferation
D0009986cellular_componentcell surface
D0010716biological_processnegative regulation of extracellular matrix disassembly
D0016020cellular_componentmembrane
D0016324cellular_componentapical plasma membrane
D0016486biological_processpeptide hormone processing
D0016787molecular_functionhydrolase activity
D0019065biological_processreceptor-mediated endocytosis of virus by host cell
D0030027cellular_componentlamellipodium
D0030139cellular_componentendocytic vesicle
D0031258cellular_componentlamellipodium membrane
D0031295biological_processT cell costimulation
D0033632biological_processregulation of cell-cell adhesion mediated by integrin
D0035641biological_processlocomotory exploration behavior
D0036343biological_processpsychomotor behavior
D0042110biological_processT cell activation
D0042802molecular_functionidentical protein binding
D0042803molecular_functionprotein homodimerization activity
D0042995cellular_componentcell projection
D0043542biological_processendothelial cell migration
D0045121cellular_componentmembrane raft
D0045499molecular_functionchemorepellent activity
D0046581cellular_componentintercellular canaliculus
D0046718biological_processsymbiont entry into host cell
D0046813biological_processreceptor-mediated virion attachment to host cell
D0050919biological_processnegative chemotaxis
D0061025biological_processmembrane fusion
D0070062cellular_componentextracellular exosome
D0070161cellular_componentanchoring junction
D0090024biological_processnegative regulation of neutrophil chemotaxis
D0120116biological_processglucagon processing
Functional Information from PDB Data
site_idAC1
Number of Residues13
Detailsbinding site for residue 8VU A 801
ChainResidue
AARG125
ATYR662
ATYR666
AASN710
AVAL711
AGLU205
AGLU206
ASER209
APHE357
ATYR547
ASER630
ATYR631
AVAL656
site_idAC2
Number of Residues13
Detailsbinding site for residue 8VU B 801
ChainResidue
BARG125
BGLU205
BGLU206
BSER209
BPHE357
BSER630
BTYR631
BVAL656
BTRP659
BTYR662
BTYR666
BASN710
BVAL711
site_idAC3
Number of Residues13
Detailsbinding site for residue 8VU C 801
ChainResidue
CARG125
CGLU205
CGLU206
CSER209
CPHE357
CTYR547
CSER630
CTYR631
CVAL656
CTYR662
CTYR666
CASN710
CVAL711
site_idAC4
Number of Residues14
Detailsbinding site for residue 8VU D 801
ChainResidue
DARG125
DGLU205
DGLU206
DSER209
DPHE357
DSER630
DTYR631
DVAL656
DTRP659
DTYR662
DTYR666
DASN710
DVAL711
DHIS740
Functional Information from PROSITE/UniProt
site_idPS00708
Number of Residues31
DetailsPRO_ENDOPEP_SER Prolyl endopeptidase family serine active site. DqieAarqFskmgfvdnkriaiwGwSyGGYV
ChainResidueDetails
AASP605-VAL635
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU10084","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues8
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12483204","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12646248","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12906826","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20684603","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23835475","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4L72","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20684603","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23835475","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4L72","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12483204","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12906826","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20684603","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23835475","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4L72","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12483204","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12646248","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20684603","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23835475","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4L72","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12483204","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12646248","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12906826","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23835475","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4L72","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12483204","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12646248","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23835475","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4L72","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12483204","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20684603","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23835475","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4L72","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 169
ChainResidueDetails
ATYR547electrostatic stabiliser, hydrogen bond donor
ASER630covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
ATYR631electrostatic stabiliser, hydrogen bond donor
AASP708activator, electrostatic stabiliser, hydrogen bond acceptor
AHIS740electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
site_idMCSA2
Number of Residues5
DetailsM-CSA 169
ChainResidueDetails
BTYR547electrostatic stabiliser, hydrogen bond donor
BSER630covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
BTYR631electrostatic stabiliser, hydrogen bond donor
BASP708activator, electrostatic stabiliser, hydrogen bond acceptor
BHIS740electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
site_idMCSA3
Number of Residues5
DetailsM-CSA 169
ChainResidueDetails
CTYR547electrostatic stabiliser, hydrogen bond donor
CSER630covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
CTYR631electrostatic stabiliser, hydrogen bond donor
CASP708activator, electrostatic stabiliser, hydrogen bond acceptor
CHIS740electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
site_idMCSA4
Number of Residues5
DetailsM-CSA 169
ChainResidueDetails
DTYR547electrostatic stabiliser, hydrogen bond donor
DSER630covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
DTYR631electrostatic stabiliser, hydrogen bond donor
DASP708activator, electrostatic stabiliser, hydrogen bond acceptor
DHIS740electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

243911

PDB entries from 2025-10-29

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