Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2ZN9

Crystal structure of Ca2+-bound form of des3-20ALG-2

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0001525	biological_process	angiogenesis
A	0001938	biological_process	positive regulation of endothelial cell proliferation
A	0005509	molecular_function	calcium ion binding
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005768	cellular_component	endosome
A	0005783	cellular_component	endoplasmic reticulum
A	0005789	cellular_component	endoplasmic reticulum membrane
A	0005829	cellular_component	cytosol
A	0006886	biological_process	intracellular protein transport
A	0006888	biological_process	endoplasmic reticulum to Golgi vesicle-mediated transport
A	0006915	biological_process	apoptotic process
A	0010595	biological_process	positive regulation of endothelial cell migration
A	0012507	cellular_component	ER to Golgi transport vesicle membrane
A	0014029	biological_process	neural crest formation
A	0014032	biological_process	neural crest cell development
A	0030127	cellular_component	COPII vesicle coat
A	0030674	molecular_function	protein-macromolecule adaptor activity
A	0030948	biological_process	negative regulation of vascular endothelial growth factor receptor signaling pathway
A	0031410	cellular_component	cytoplasmic vesicle
A	0031463	cellular_component	Cul3-RING ubiquitin ligase complex
A	0032007	biological_process	negative regulation of TOR signaling
A	0034605	biological_process	cellular response to heat
A	0036324	biological_process	vascular endothelial growth factor receptor-2 signaling pathway
A	0042802	molecular_function	identical protein binding
A	0042803	molecular_function	protein homodimerization activity
A	0043065	biological_process	positive regulation of apoptotic process
A	0043495	molecular_function	protein-membrane adaptor activity
A	0045766	biological_process	positive regulation of angiogenesis
A	0046872	molecular_function	metal ion binding
A	0046982	molecular_function	protein heterodimerization activity
A	0046983	molecular_function	protein dimerization activity
A	0048208	biological_process	COPII vesicle coating
A	0048306	molecular_function	calcium-dependent protein binding
A	0048471	cellular_component	perinuclear region of cytoplasm
A	0051592	biological_process	response to calcium ion
A	0051898	biological_process	negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
A	0070062	cellular_component	extracellular exosome
A	0070971	cellular_component	endoplasmic reticulum exit site
A	0097190	biological_process	apoptotic signaling pathway
A	1902527	biological_process	positive regulation of protein monoubiquitination
A	1990756	molecular_function	ubiquitin-like ligase-substrate adaptor activity
B	0000287	molecular_function	magnesium ion binding
B	0001525	biological_process	angiogenesis
B	0001938	biological_process	positive regulation of endothelial cell proliferation
B	0005509	molecular_function	calcium ion binding
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005654	cellular_component	nucleoplasm
B	0005737	cellular_component	cytoplasm
B	0005768	cellular_component	endosome
B	0005783	cellular_component	endoplasmic reticulum
B	0005789	cellular_component	endoplasmic reticulum membrane
B	0005829	cellular_component	cytosol
B	0006886	biological_process	intracellular protein transport
B	0006888	biological_process	endoplasmic reticulum to Golgi vesicle-mediated transport
B	0006915	biological_process	apoptotic process
B	0010595	biological_process	positive regulation of endothelial cell migration
B	0012507	cellular_component	ER to Golgi transport vesicle membrane
B	0014029	biological_process	neural crest formation
B	0014032	biological_process	neural crest cell development
B	0030127	cellular_component	COPII vesicle coat
B	0030674	molecular_function	protein-macromolecule adaptor activity
B	0030948	biological_process	negative regulation of vascular endothelial growth factor receptor signaling pathway
B	0031410	cellular_component	cytoplasmic vesicle
B	0031463	cellular_component	Cul3-RING ubiquitin ligase complex
B	0032007	biological_process	negative regulation of TOR signaling
B	0034605	biological_process	cellular response to heat
B	0036324	biological_process	vascular endothelial growth factor receptor-2 signaling pathway
B	0042802	molecular_function	identical protein binding
B	0042803	molecular_function	protein homodimerization activity
B	0043065	biological_process	positive regulation of apoptotic process
B	0043495	molecular_function	protein-membrane adaptor activity
B	0045766	biological_process	positive regulation of angiogenesis
B	0046872	molecular_function	metal ion binding
B	0046982	molecular_function	protein heterodimerization activity
B	0046983	molecular_function	protein dimerization activity
B	0048208	biological_process	COPII vesicle coating
B	0048306	molecular_function	calcium-dependent protein binding
B	0048471	cellular_component	perinuclear region of cytoplasm
B	0051592	biological_process	response to calcium ion
B	0051898	biological_process	negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
B	0070062	cellular_component	extracellular exosome
B	0070971	cellular_component	endoplasmic reticulum exit site
B	0097190	biological_process	apoptotic signaling pathway
B	1902527	biological_process	positive regulation of protein monoubiquitination
B	1990756	molecular_function	ubiquitin-like ligase-substrate adaptor activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 901

Chain	Residue
A	ASP36
A	ASP38
A	SER40
A	VAL42
A	GLU47
A	HOH927

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA A 902

Chain	Residue
A	MET109
A	GLU114
A	ASP103
A	ASP105
A	SER107

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 903

Chain	Residue
A	ASP169
A	ASP171
A	ASP173
A	TRP175
A	HOH924
A	HOH928

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA A 904

Chain	Residue
A	ASN106
A	HOH920
B	ASN106
B	HOH924

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE 2PE A 1

Chain	Residue
A	TYR91
A	TRP95
A	PHE122
A	GLY123
A	TYR124
A	ARG166
B	PRO23
B	GLN25

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA B 901

Chain	Residue
B	ASP36
B	ASP38
B	SER40
B	VAL42
B	GLU47
B	HOH915

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA B 902

Chain	Residue
B	ASP103
B	ASP105
B	SER107
B	MET109
B	GLU114

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA B 903

Chain	Residue
B	ASP169
B	ASP171
B	ASP173
B	TRP175
B	HOH914
B	HOH925

site_id	AC9
Number of Residues	11
Details	BINDING SITE FOR RESIDUE 12P B 2

Chain	Residue
A	ALA21
A	PRO23
A	GLN25
A	LEU28
A	THR86
B	TYR91
B	ASP94
B	TRP95
B	GLY123
B	TYR124
B	ARG166

Functional Information from PROSITE/UniProt

site_id	PS00018
Number of Residues	13
Details	EF_HAND_1 EF-hand calcium-binding domain. DKDRSGVISdtEL

Chain	Residue	Details
A	ASP36-LEU48
A	ASP103-LEU115

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	70
Details	Domain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	60
Details	Domain: {"description":"EF-hand 2","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	70
Details	Domain: {"description":"EF-hand 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	70
Details	Domain: {"description":"EF-hand 4","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18940611","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18997320","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20691033","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25667979","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18940611","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18997320","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20691033","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25667979","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P12815","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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