6VII

Crystal structure of mouse RABL3 in complex with GTPgammaS

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0001779	biological_process	natural killer cell differentiation
A	0003924	molecular_function	GTPase activity
A	0003925	molecular_function	G protein activity
A	0005515	molecular_function	protein binding
A	0005525	molecular_function	GTP binding
A	0005794	cellular_component	Golgi apparatus
A	0005813	cellular_component	centrosome
A	0006886	biological_process	intracellular protein transport
A	0012505	cellular_component	endomembrane system
A	0016787	molecular_function	hydrolase activity
A	0030183	biological_process	B cell differentiation
A	0033077	biological_process	T cell differentiation in thymus
A	0042803	molecular_function	protein homodimerization activity
A	0045724	biological_process	positive regulation of cilium assembly
A	0046578	biological_process	regulation of Ras protein signal transduction
A	0050821	biological_process	protein stabilization
A	1903059	biological_process	regulation of protein lipidation
B	0000166	molecular_function	nucleotide binding
B	0001779	biological_process	natural killer cell differentiation
B	0003924	molecular_function	GTPase activity
B	0003925	molecular_function	G protein activity
B	0005515	molecular_function	protein binding
B	0005525	molecular_function	GTP binding
B	0005794	cellular_component	Golgi apparatus
B	0005813	cellular_component	centrosome
B	0006886	biological_process	intracellular protein transport
B	0012505	cellular_component	endomembrane system
B	0016787	molecular_function	hydrolase activity
B	0030183	biological_process	B cell differentiation
B	0033077	biological_process	T cell differentiation in thymus
B	0042803	molecular_function	protein homodimerization activity
B	0045724	biological_process	positive regulation of cilium assembly
B	0046578	biological_process	regulation of Ras protein signal transduction
B	0050821	biological_process	protein stabilization
B	1903059	biological_process	regulation of protein lipidation

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue MG B 301

Chain	Residue
B	SER20
B	THR38
B	GSP302
B	HOH411
B	HOH423

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site_id	AC2
Number of Residues	21
Details	binding site for residue GSP B 302

Chain	Residue
B	LYS19
B	SER20
B	SER21
B	PRO35
B	THR38
B	LYS148
B	ASP150
B	GLN151
B	ASP179
B	CYS180
B	THR181
B	MG301
B	HOH407
B	HOH411
B	HOH412
B	HOH423
B	HOH428
B	SER15
B	GLY16
B	VAL17
B	GLY18

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site_id	AC3
Number of Residues	5
Details	binding site for residue MG A 301

Chain	Residue
A	SER20
A	THR38
A	GSP302
A	HOH404
A	HOH412

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site_id	AC4
Number of Residues	22
Details	binding site for residue GSP A 302

Chain	Residue
A	SER15
A	GLY16
A	VAL17
A	GLY18
A	LYS19
A	SER20
A	SER21
A	PRO35
A	THR38
A	LYS148
A	ASP150
A	ASP179
A	CYS180
A	THR181
A	MG301
A	HOH402
A	HOH404
A	HOH407
A	HOH412
A	HOH414
A	HOH434
A	HOH452

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Functional Information from PROSITE/UniProt

site_id	PS00675
Number of Residues	14
Details	SIGMA54_INTERACT_1 Sigma-54 interaction domain ATP-binding region A signature. VLVlGDSGVGKssL

Chain	Residue	Details
B	VAL9-LEU22

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"32220963","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6VII","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6VIJ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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