3VLC

Crystal structure of S. cerevisiae Get3 in the semi open conformation in complex with Get1 cytosolic domain at 4.5 angstrom resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000750	biological_process	pheromone-dependent signal transduction involved in conjugation with cellular fusion
A	0005085	molecular_function	guanyl-nucleotide exchange factor activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005783	cellular_component	endoplasmic reticulum
A	0005789	cellular_component	endoplasmic reticulum membrane
A	0005794	cellular_component	Golgi apparatus
A	0005829	cellular_component	cytosol
A	0006457	biological_process	protein folding
A	0006620	biological_process	post-translational protein targeting to endoplasmic reticulum membrane
A	0006890	biological_process	retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum
A	0008270	molecular_function	zinc ion binding
A	0009408	biological_process	response to heat
A	0010038	biological_process	response to metal ion
A	0016192	biological_process	vesicle-mediated transport
A	0016787	molecular_function	hydrolase activity
A	0016887	molecular_function	ATP hydrolysis activity
A	0034599	biological_process	cellular response to oxidative stress
A	0042802	molecular_function	identical protein binding
A	0043529	cellular_component	GET complex
A	0044183	molecular_function	protein folding chaperone
A	0045048	biological_process	protein insertion into ER membrane
A	0046685	biological_process	response to arsenic-containing substance
A	0046872	molecular_function	metal ion binding
A	0051082	molecular_function	unfolded protein binding
A	0071816	biological_process	tail-anchored membrane protein insertion into ER membrane
E	0071816	biological_process	tail-anchored membrane protein insertion into ER membrane

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ADP A 401

Chain	Residue
A	GLY27
A	PRO315
A	LEU316
A	CYS317
A	GLU320
A	ILE321
A	ARG322
A	PHE330
E	GLN62
A	GLY28
A	VAL29
A	GLY30
A	LYS31
A	THR32
A	THR33
A	LEU247
A	ASN272

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE:

Chain	Residue	Details
A	ASP57

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING:

Chain	Residue	Details
A	LYS26
A	GLU245
A	ASN272
A	PRO315

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03112, ECO:0000269|PubMed:19675567

Chain	Residue	Details
A	CYS285
A	CYS288

---