5CJO

Crystal Structure Analysis of Elbow-Engineered-Fab-Bound Human Insulin Degrading Enzyme (IDE) in Complex with Insulin

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
a	0005179	molecular_function	hormone activity
a	0005576	cellular_component	extracellular region

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue EPE A 2001

Chain	Residue
A	ARG839
A	ALA840
A	ASN841
A	GLY842
A	ARG893
A	SER913

---

site_id	AC2
Number of Residues	4
Details	binding site for residue ZN A 2002

Chain	Residue
a	TYR14
A	HIS108
A	HIS112
A	GLU189

---

Functional Information from PROSITE/UniProt

site_id	PS00262
Number of Residues	15
Details	INSULIN Insulin family signature. CCTSiCSlyqLenyC

Chain	Residue	Details
a	CYS6-CYS20

---

site_id	PS00290
Number of Residues	7
Details	IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YICNVNH

Chain	Residue	Details
H	TYR212-HIS218
L	TYR194-HIS200

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	5
Details	Motif: {"description":"SlyX motif","evidences":[{"source":"UniProtKB","id":"Q9JHR7","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
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	3
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	6
Details	Binding site: {"description":"in the exosite"}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18986166","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	7
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P35559","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9JHR7","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---