Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3E4A

Human IDE-inhibitor complex at 2.6 angstrom resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0001540	molecular_function	amyloid-beta binding
A	0001618	molecular_function	virus receptor activity
A	0003824	molecular_function	catalytic activity
A	0004175	molecular_function	endopeptidase activity
A	0004222	molecular_function	metalloendopeptidase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005777	cellular_component	peroxisome
A	0005782	cellular_component	peroxisomal matrix
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0006508	biological_process	proteolysis
A	0008233	molecular_function	peptidase activity
A	0008237	molecular_function	metallopeptidase activity
A	0008270	molecular_function	zinc ion binding
A	0008286	biological_process	insulin receptor signaling pathway
A	0009897	cellular_component	external side of plasma membrane
A	0009986	cellular_component	cell surface
A	0010815	biological_process	bradykinin catabolic process
A	0010992	biological_process	ubiquitin recycling
A	0016323	cellular_component	basolateral plasma membrane
A	0016787	molecular_function	hydrolase activity
A	0016887	molecular_function	ATP hydrolysis activity
A	0017046	molecular_function	peptide hormone binding
A	0019885	biological_process	antigen processing and presentation of endogenous peptide antigen via MHC class I
A	0030163	biological_process	protein catabolic process
A	0031597	cellular_component	cytosolic proteasome complex
A	0031626	molecular_function	beta-endorphin binding
A	0032092	biological_process	positive regulation of protein binding
A	0042277	molecular_function	peptide binding
A	0042447	biological_process	hormone catabolic process
A	0042802	molecular_function	identical protein binding
A	0042803	molecular_function	protein homodimerization activity
A	0043171	biological_process	peptide catabolic process
A	0043559	molecular_function	insulin binding
A	0044877	molecular_function	protein-containing complex binding
A	0045732	biological_process	positive regulation of protein catabolic process
A	0045861	biological_process	negative regulation of proteolysis
A	0046718	biological_process	symbiont entry into host cell
A	0046872	molecular_function	metal ion binding
A	0050435	biological_process	amyloid-beta metabolic process
A	0051603	biological_process	proteolysis involved in protein catabolic process
A	0070062	cellular_component	extracellular exosome
A	0097242	biological_process	amyloid-beta clearance
A	0150094	biological_process	amyloid-beta clearance by cellular catabolic process
A	1901142	biological_process	insulin metabolic process
A	1901143	biological_process	insulin catabolic process
A	1903715	biological_process	regulation of aerobic respiration
B	0000166	molecular_function	nucleotide binding
B	0001540	molecular_function	amyloid-beta binding
B	0001618	molecular_function	virus receptor activity
B	0003824	molecular_function	catalytic activity
B	0004175	molecular_function	endopeptidase activity
B	0004222	molecular_function	metalloendopeptidase activity
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005576	cellular_component	extracellular region
B	0005615	cellular_component	extracellular space
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005739	cellular_component	mitochondrion
B	0005777	cellular_component	peroxisome
B	0005782	cellular_component	peroxisomal matrix
B	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0006508	biological_process	proteolysis
B	0008233	molecular_function	peptidase activity
B	0008237	molecular_function	metallopeptidase activity
B	0008270	molecular_function	zinc ion binding
B	0008286	biological_process	insulin receptor signaling pathway
B	0009897	cellular_component	external side of plasma membrane
B	0009986	cellular_component	cell surface
B	0010815	biological_process	bradykinin catabolic process
B	0010992	biological_process	ubiquitin recycling
B	0016323	cellular_component	basolateral plasma membrane
B	0016787	molecular_function	hydrolase activity
B	0016887	molecular_function	ATP hydrolysis activity
B	0017046	molecular_function	peptide hormone binding
B	0019885	biological_process	antigen processing and presentation of endogenous peptide antigen via MHC class I
B	0030163	biological_process	protein catabolic process
B	0031597	cellular_component	cytosolic proteasome complex
B	0031626	molecular_function	beta-endorphin binding
B	0032092	biological_process	positive regulation of protein binding
B	0042277	molecular_function	peptide binding
B	0042447	biological_process	hormone catabolic process
B	0042802	molecular_function	identical protein binding
B	0042803	molecular_function	protein homodimerization activity
B	0043171	biological_process	peptide catabolic process
B	0043559	molecular_function	insulin binding
B	0044877	molecular_function	protein-containing complex binding
B	0045732	biological_process	positive regulation of protein catabolic process
B	0045861	biological_process	negative regulation of proteolysis
B	0046718	biological_process	symbiont entry into host cell
B	0046872	molecular_function	metal ion binding
B	0050435	biological_process	amyloid-beta metabolic process
B	0051603	biological_process	proteolysis involved in protein catabolic process
B	0070062	cellular_component	extracellular exosome
B	0097242	biological_process	amyloid-beta clearance
B	0150094	biological_process	amyloid-beta clearance by cellular catabolic process
B	1901142	biological_process	insulin metabolic process
B	1901143	biological_process	insulin catabolic process
B	1903715	biological_process	regulation of aerobic respiration

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 2000

Chain	Residue
A	HIS108
A	HIS112
A	GLU189
A	QIX2001

site_id	AC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE QIX A 2001

Chain	Residue
A	ASN139
A	ALA140
A	GLU189
A	PHE820
A	ARG824
A	TYR831
A	ZN2000
A	HIS108
A	GLN111
A	HIS112
A	LEU116
A	SER128

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE DIO A 2002

Chain	Residue
A	GLN800
A	GLU910
A	SER913
A	ARG920
A	DIO2003

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE DIO A 2003

Chain	Residue
A	GLN800
A	ARG839
A	ALA840
A	ASN841
A	GLY842
A	DIO2002

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE ACY A 2004

Chain	Residue
A	LYS558
A	TYR916

site_id	AC6
Number of Residues	1
Details	BINDING SITE FOR RESIDUE ACY A 2005

Chain	Residue
A	LYS120

site_id	AC7
Number of Residues	1
Details	BINDING SITE FOR RESIDUE ACY A 2006

Chain	Residue
A	GLU290

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ACY A 2007

Chain	Residue
A	GLU465
A	PRO639
A	MET744

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ACY A 2008

Chain	Residue
A	GLU990
A	PHE998
A	GLY1001
A	LEU1002

site_id	BC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE ACY A 2009

Chain	Residue
A	GLU529

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACY A 2010

Chain	Residue
A	ASN312
A	THR358
A	VAL360
A	VAL377
A	ASP378

site_id	BC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE ACY A 2011

Chain	Residue
A	LEU204

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 2000

Chain	Residue
B	HIS108
B	HIS112
B	GLU189
B	QIX2001

site_id	BC5
Number of Residues	15
Details	BINDING SITE FOR RESIDUE QIX B 2001

Chain	Residue
B	HIS108
B	GLN111
B	HIS112
B	LEU116
B	SER128
B	ASN139
B	ALA140
B	GLU182
B	GLU189
B	PHE820
B	ARG824
B	TYR831
B	ZN2000
B	HOH2160
B	HOH2164

site_id	BC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE DIO B 2002

Chain	Residue
B	LEU201
B	LEU204
B	GLU205
B	THR208
B	ARG477
B	ALA479
B	HOH2018
B	HOH2054

site_id	BC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE DIO B 2003

Chain	Residue
B	GLN800
B	ARG839
B	ALA840
B	ASN841
B	SER913
B	DIO2004

site_id	BC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE DIO B 2004

Chain	Residue
B	SER913
B	DIO2003

site_id	BC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE DIO B 2005

Chain	Residue
B	LEU170
B	HIS245

site_id	CC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE DIO B 2006

Chain	Residue
B	ASP698
B	TYR779

site_id	CC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ACY B 2007

Chain	Residue
B	GLY775
B	TRP776
B	GLU990

site_id	CC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ACY B 2008

Chain	Residue
B	LYS212
B	HIS213
B	PRO214
B	GLU290

site_id	CC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE ACY B 2009

Chain	Residue
B	GLU529

site_id	CC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE ACY B 2010

Chain	Residue
B	THR358
B	VAL377

site_id	CC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ACY B 2011

Chain	Residue
A	LYS1009
B	GLU990
B	PHE998
B	GLY1001

site_id	CC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE ACY B 2012

Chain	Residue
B	TRP513
B	LEU301

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	10
Details	Motif: {"description":"SlyX motif","evidences":[{"source":"UniProtKB","id":"Q9JHR7","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10096","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10684867","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"17051221","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"19321446","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"23922390","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10096","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17051221","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17613531","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18986166","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19321446","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2G54","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2JG4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CWW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3N56","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3N57","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	12
Details	Binding site: {"description":"in the exosite"}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18986166","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	14
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P35559","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	4
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9JHR7","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1hr6

Chain	Residue	Details
A	GLN111

site_id	CSA2
Number of Residues	1
Details	Annotated By Reference To The Literature 1hr6

Chain	Residue	Details
B	GLN111

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