Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4LKO

Crystal structure of human DPP-IV in complex with BMS-744891

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001618	molecular_function	virus receptor activity
A	0001662	biological_process	behavioral fear response
A	0001666	biological_process	response to hypoxia
A	0002020	molecular_function	protease binding
A	0004177	molecular_function	aminopeptidase activity
A	0004252	molecular_function	serine-type endopeptidase activity
A	0005102	molecular_function	signaling receptor binding
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005765	cellular_component	lysosomal membrane
A	0005886	cellular_component	plasma membrane
A	0005925	cellular_component	focal adhesion
A	0006508	biological_process	proteolysis
A	0007155	biological_process	cell adhesion
A	0008233	molecular_function	peptidase activity
A	0008236	molecular_function	serine-type peptidase activity
A	0008239	molecular_function	dipeptidyl-peptidase activity
A	0008284	biological_process	positive regulation of cell population proliferation
A	0009986	cellular_component	cell surface
A	0010716	biological_process	negative regulation of extracellular matrix disassembly
A	0016020	cellular_component	membrane
A	0016324	cellular_component	apical plasma membrane
A	0016486	biological_process	peptide hormone processing
A	0016787	molecular_function	hydrolase activity
A	0019065	biological_process	receptor-mediated endocytosis of virus by host cell
A	0030027	cellular_component	lamellipodium
A	0030139	cellular_component	endocytic vesicle
A	0031258	cellular_component	lamellipodium membrane
A	0031295	biological_process	T cell costimulation
A	0033632	biological_process	regulation of cell-cell adhesion mediated by integrin
A	0035641	biological_process	locomotory exploration behavior
A	0036343	biological_process	psychomotor behavior
A	0042110	biological_process	T cell activation
A	0042802	molecular_function	identical protein binding
A	0042803	molecular_function	protein homodimerization activity
A	0042995	cellular_component	cell projection
A	0043542	biological_process	endothelial cell migration
A	0045121	cellular_component	membrane raft
A	0045499	molecular_function	chemorepellent activity
A	0046581	cellular_component	intercellular canaliculus
A	0046718	biological_process	symbiont entry into host cell
A	0046813	biological_process	receptor-mediated virion attachment to host cell
A	0050919	biological_process	negative chemotaxis
A	0061025	biological_process	membrane fusion
A	0070062	cellular_component	extracellular exosome
A	0070161	cellular_component	anchoring junction
A	0090024	biological_process	negative regulation of neutrophil chemotaxis
A	0120116	biological_process	glucagon processing
B	0001618	molecular_function	virus receptor activity
B	0001662	biological_process	behavioral fear response
B	0001666	biological_process	response to hypoxia
B	0002020	molecular_function	protease binding
B	0004177	molecular_function	aminopeptidase activity
B	0004252	molecular_function	serine-type endopeptidase activity
B	0005102	molecular_function	signaling receptor binding
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005765	cellular_component	lysosomal membrane
B	0005886	cellular_component	plasma membrane
B	0005925	cellular_component	focal adhesion
B	0006508	biological_process	proteolysis
B	0007155	biological_process	cell adhesion
B	0008233	molecular_function	peptidase activity
B	0008236	molecular_function	serine-type peptidase activity
B	0008239	molecular_function	dipeptidyl-peptidase activity
B	0008284	biological_process	positive regulation of cell population proliferation
B	0009986	cellular_component	cell surface
B	0010716	biological_process	negative regulation of extracellular matrix disassembly
B	0016020	cellular_component	membrane
B	0016324	cellular_component	apical plasma membrane
B	0016486	biological_process	peptide hormone processing
B	0016787	molecular_function	hydrolase activity
B	0019065	biological_process	receptor-mediated endocytosis of virus by host cell
B	0030027	cellular_component	lamellipodium
B	0030139	cellular_component	endocytic vesicle
B	0031258	cellular_component	lamellipodium membrane
B	0031295	biological_process	T cell costimulation
B	0033632	biological_process	regulation of cell-cell adhesion mediated by integrin
B	0035641	biological_process	locomotory exploration behavior
B	0036343	biological_process	psychomotor behavior
B	0042110	biological_process	T cell activation
B	0042802	molecular_function	identical protein binding
B	0042803	molecular_function	protein homodimerization activity
B	0042995	cellular_component	cell projection
B	0043542	biological_process	endothelial cell migration
B	0045121	cellular_component	membrane raft
B	0045499	molecular_function	chemorepellent activity
B	0046581	cellular_component	intercellular canaliculus
B	0046718	biological_process	symbiont entry into host cell
B	0046813	biological_process	receptor-mediated virion attachment to host cell
B	0050919	biological_process	negative chemotaxis
B	0061025	biological_process	membrane fusion
B	0070062	cellular_component	extracellular exosome
B	0070161	cellular_component	anchoring junction
B	0090024	biological_process	negative regulation of neutrophil chemotaxis
B	0120116	biological_process	glucagon processing

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE 1WH A 801

Chain	Residue
A	GLU205
A	GLU206
A	TYR547
A	SER630
A	VAL656
A	TYR662
A	TYR666
A	ASN710
A	HIS740

site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE 1WH B 801

Chain	Residue
B	ARG125
B	GLU205
B	GLU206
B	TYR547
B	SER630
B	VAL656
B	TYR662
B	TYR666
B	ASN710
B	HIS740

Functional Information from PROSITE/UniProt

site_id	PS00708
Number of Residues	31
Details	PRO_ENDOPEP_SER Prolyl endopeptidase family serine active site. DqieAarqFskmgfvdnkriaiwGwSyGGYV

Chain	Residue	Details
A	ASP605-VAL635

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Active site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU10084","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Glycosylation: {"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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	2
Details	Glycosylation: {"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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Glycosylation: {"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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Glycosylation: {"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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	2
Details	Glycosylation: {"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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Glycosylation: {"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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	2
Details	Glycosylation: {"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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	5
Details	M-CSA 169

Chain	Residue	Details
A	TYR547	electrostatic stabiliser, hydrogen bond donor
A	SER630	covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
A	TYR631	electrostatic stabiliser, hydrogen bond donor
A	ASP708	activator, electrostatic stabiliser, hydrogen bond acceptor
A	HIS740	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_id	MCSA2
Number of Residues	5
Details	M-CSA 169

Chain	Residue	Details
B	TYR547	electrostatic stabiliser, hydrogen bond donor
B	SER630	covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
B	TYR631	electrostatic stabiliser, hydrogen bond donor
B	ASP708	activator, electrostatic stabiliser, hydrogen bond acceptor
B	HIS740	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)