Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2AJL

X-ray Structure of Novel Biaryl-Based Dipeptidyl peptidase IV inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
I0001618molecular_functionvirus receptor activity
I0001662biological_processbehavioral fear response
I0001666biological_processresponse to hypoxia
I0002020molecular_functionprotease binding
I0004177molecular_functionaminopeptidase activity
I0004252molecular_functionserine-type endopeptidase activity
I0005102molecular_functionsignaling receptor binding
I0005515molecular_functionprotein binding
I0005576cellular_componentextracellular region
I0005765cellular_componentlysosomal membrane
I0005886cellular_componentplasma membrane
I0005925cellular_componentfocal adhesion
I0006508biological_processproteolysis
I0007155biological_processcell adhesion
I0008233molecular_functionpeptidase activity
I0008236molecular_functionserine-type peptidase activity
I0008239molecular_functiondipeptidyl-peptidase activity
I0008284biological_processpositive regulation of cell population proliferation
I0009986cellular_componentcell surface
I0010716biological_processnegative regulation of extracellular matrix disassembly
I0016020cellular_componentmembrane
I0016324cellular_componentapical plasma membrane
I0016486biological_processpeptide hormone processing
I0016787molecular_functionhydrolase activity
I0019065biological_processreceptor-mediated endocytosis of virus by host cell
I0030027cellular_componentlamellipodium
I0030139cellular_componentendocytic vesicle
I0031258cellular_componentlamellipodium membrane
I0031295biological_processT cell costimulation
I0033632biological_processregulation of cell-cell adhesion mediated by integrin
I0035641biological_processlocomotory exploration behavior
I0036343biological_processpsychomotor behavior
I0042110biological_processT cell activation
I0042802molecular_functionidentical protein binding
I0042803molecular_functionprotein homodimerization activity
I0042995cellular_componentcell projection
I0043542biological_processendothelial cell migration
I0045121cellular_componentmembrane raft
I0045499molecular_functionchemorepellent activity
I0046581cellular_componentintercellular canaliculus
I0046718biological_processsymbiont entry into host cell
I0046813biological_processreceptor-mediated virion attachment to host cell
I0050919biological_processnegative chemotaxis
I0061025biological_processmembrane fusion
I0070062cellular_componentextracellular exosome
I0070161cellular_componentanchoring junction
I0090024biological_processnegative regulation of neutrophil chemotaxis
I0120116biological_processglucagon processing
J0001618molecular_functionvirus receptor activity
J0001662biological_processbehavioral fear response
J0001666biological_processresponse to hypoxia
J0002020molecular_functionprotease binding
J0004177molecular_functionaminopeptidase activity
J0004252molecular_functionserine-type endopeptidase activity
J0005102molecular_functionsignaling receptor binding
J0005515molecular_functionprotein binding
J0005576cellular_componentextracellular region
J0005765cellular_componentlysosomal membrane
J0005886cellular_componentplasma membrane
J0005925cellular_componentfocal adhesion
J0006508biological_processproteolysis
J0007155biological_processcell adhesion
J0008233molecular_functionpeptidase activity
J0008236molecular_functionserine-type peptidase activity
J0008239molecular_functiondipeptidyl-peptidase activity
J0008284biological_processpositive regulation of cell population proliferation
J0009986cellular_componentcell surface
J0010716biological_processnegative regulation of extracellular matrix disassembly
J0016020cellular_componentmembrane
J0016324cellular_componentapical plasma membrane
J0016486biological_processpeptide hormone processing
J0016787molecular_functionhydrolase activity
J0019065biological_processreceptor-mediated endocytosis of virus by host cell
J0030027cellular_componentlamellipodium
J0030139cellular_componentendocytic vesicle
J0031258cellular_componentlamellipodium membrane
J0031295biological_processT cell costimulation
J0033632biological_processregulation of cell-cell adhesion mediated by integrin
J0035641biological_processlocomotory exploration behavior
J0036343biological_processpsychomotor behavior
J0042110biological_processT cell activation
J0042802molecular_functionidentical protein binding
J0042803molecular_functionprotein homodimerization activity
J0042995cellular_componentcell projection
J0043542biological_processendothelial cell migration
J0045121cellular_componentmembrane raft
J0045499molecular_functionchemorepellent activity
J0046581cellular_componentintercellular canaliculus
J0046718biological_processsymbiont entry into host cell
J0046813biological_processreceptor-mediated virion attachment to host cell
J0050919biological_processnegative chemotaxis
J0061025biological_processmembrane fusion
J0070062cellular_componentextracellular exosome
J0070161cellular_componentanchoring junction
J0090024biological_processnegative regulation of neutrophil chemotaxis
J0120116biological_processglucagon processing
Functional Information from PROSITE/UniProt
site_idPS00708
Number of Residues31
DetailsPRO_ENDOPEP_SER Prolyl endopeptidase family serine active site. DqieAarqFskmgfvdnkriaiwGwSyGGYV
ChainResidueDetails
IASP605-VAL635

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084
ChainResidueDetails
ISER630
IASP708
IHIS740
JSER630
JASP708
JHIS740

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
IASN85
IASN229
JASN85
JASN229

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
IASN92
JASN92

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
IASN150
JASN150

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
IASN219
JASN219

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
IASN281
JASN281

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
IASN321
JASN321

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
IASN520
JASN520

site_idSWS_FT_FI9
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218
ChainResidueDetails
IASN685
JASN685

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1jkm
ChainResidueDetails
IHIS740
IASP708
ISER630

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1jkm
ChainResidueDetails
JHIS740
JASP708
JSER630

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1jkm
ChainResidueDetails
IHIS740
ISER630
IASP709

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1jkm
ChainResidueDetails
JHIS740
JSER630
JASP709

site_idMCSA1
Number of Residues5
DetailsM-CSA 169
ChainResidueDetails

site_idMCSA2
Number of Residues5
DetailsM-CSA 169
ChainResidueDetails

237735

PDB entries from 2025-06-18

PDB statisticsPDBj update infoContact PDBjnumon