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2G5P

Crystal structure of human dipeptidyl peptidase IV (DPPIV) complexed with cyanopyrrolidine (C5-pro-pro) inhibitor 21ac

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
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE ADF A 800
ChainResidue
AGLU205
AASN710
AHOH984
AHOH1347
AGLU206
ASER209
ATYR547
ASER630
ATYR631
AVAL656
ATYR662
ATYR666

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 Residues6
DetailsACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084
ChainResidueDetails
ASER630
AASP708
AHIS740
BSER630
BASP708
BHIS740

site_idSWS_FT_FI2
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
ChainResidueDetails
AASN85
AASN229
BASN85
BASN229

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
ChainResidueDetails
AASN92
BASN92

site_idSWS_FT_FI4
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
ChainResidueDetails
AASN150
BASN150

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
ChainResidueDetails
AASN219
BASN219

site_idSWS_FT_FI6
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
ChainResidueDetails
AASN281
BASN281

site_idSWS_FT_FI7
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
ChainResidueDetails
AASN321
BASN321

site_idSWS_FT_FI8
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
ChainResidueDetails
AASN520
BASN520

site_idSWS_FT_FI9
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218
ChainResidueDetails
AASN685
BASN685

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

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PDB entries from 2024-03-27

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