Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1YHN

Structure basis of RILP recruitment by Rab7

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000045	biological_process	autophagosome assembly
A	0000166	molecular_function	nucleotide binding
A	0000421	cellular_component	autophagosome membrane
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	0005739	cellular_component	mitochondrion
A	0005764	cellular_component	lysosome
A	0005765	cellular_component	lysosomal membrane
A	0005770	cellular_component	late endosome
A	0005811	cellular_component	lipid droplet
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0006622	biological_process	protein targeting to lysosome
A	0006629	biological_process	lipid metabolic process
A	0006897	biological_process	endocytosis
A	0006914	biological_process	autophagy
A	0007174	biological_process	epidermal growth factor catabolic process
A	0008333	biological_process	endosome to lysosome transport
A	0009617	biological_process	response to bacterium
A	0010008	cellular_component	endosome membrane
A	0015031	biological_process	protein transport
A	0016042	biological_process	lipid catabolic process
A	0016787	molecular_function	hydrolase activity
A	0019003	molecular_function	GDP binding
A	0019076	biological_process	viral release from host cell
A	0022615	biological_process	protein to membrane docking
A	0030667	cellular_component	secretory granule membrane
A	0030670	cellular_component	phagocytic vesicle membrane
A	0030672	cellular_component	synaptic vesicle membrane
A	0030904	cellular_component	retromer complex
A	0031267	molecular_function	small GTPase binding
A	0031410	cellular_component	cytoplasmic vesicle
A	0031902	cellular_component	late endosome membrane
A	0031966	cellular_component	mitochondrial membrane
A	0032935	molecular_function	sterol sensor activity
A	0032991	cellular_component	protein-containing complex
A	0033162	cellular_component	melanosome membrane
A	0034045	cellular_component	phagophore assembly site membrane
A	0036466	biological_process	synaptic vesicle recycling via endosome
A	0042147	biological_process	retrograde transport, endosome to Golgi
A	0042632	biological_process	cholesterol homeostasis
A	0045022	biological_process	early endosome to late endosome transport
A	0045335	cellular_component	phagocytic vesicle
A	0045453	biological_process	bone resorption
A	0045732	biological_process	positive regulation of protein catabolic process
A	0048524	biological_process	positive regulation of viral process
A	0061462	biological_process	protein localization to lysosome
A	0061724	biological_process	lipophagy
A	0070062	cellular_component	extracellular exosome
A	0090120	biological_process	lysosome to ER cholesterol transport
A	0090382	biological_process	phagosome maturation
A	0090383	biological_process	phagosome acidification
A	0090385	biological_process	phagosome-lysosome fusion
A	0097208	cellular_component	alveolar lamellar body
A	0098588	cellular_component	bounding membrane of organelle
A	0098830	cellular_component	presynaptic endosome
A	0099638	biological_process	endosome to plasma membrane protein transport
A	1903542	biological_process	negative regulation of exosomal secretion
A	1903543	biological_process	positive regulation of exosomal secretion
A	1905366	biological_process	negative regulation of intralumenal vesicle formation
A	1905394	molecular_function	retromer complex binding
B	0046983	molecular_function	protein dimerization activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 302

Chain	Residue
A	THR22
A	THR40
A	ASP63
A	THR64
A	GTP301

site_id	AC2
Number of Residues	24
Details	BINDING SITE FOR RESIDUE GTP A 301

Chain	Residue
A	LYS21
A	THR22
A	SER23
A	PHE33
A	SER34
A	ASN35
A	TYR37
A	THR40
A	THR64
A	ALA65
A	GLY66
A	ASN125
A	LYS126
A	ASP128
A	LEU129
A	SER155
A	ALA156
A	LYS157
A	MG302
A	HOH311
A	SER17
A	GLY18
A	VAL19
A	GLY20

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. VIIlGDSGVGKtsL

Chain	Residue	Details
A	VAL11-LEU24

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	13
Details	Motif: {"description":"Switch 1","evidences":[{"source":"PubMed","id":"15933719","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1T91","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1YHN","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	15
Details	Motif: {"description":"Switch 2","evidences":[{"source":"PubMed","id":"15933719","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1T91","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1YHN","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"20028791","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3LAW","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	11
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15933719","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20028791","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1T91","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1YHN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3LAW","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15933719","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20028791","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1T91","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1YHN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3LAW","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15933719","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1YHN","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15933719","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20028791","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1YHN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3LAW","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by LRRK1","evidences":[{"source":"PubMed","id":"36040231","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"37857821","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

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

Chain	Residue	Details
A	LEU67

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

Chain	Residue	Details
A	GLY18

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