3TKL

Crystal structure of the GTP-bound Rab1a in complex with the coiled-coil domain of LidA from Legionella pneumophila

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000045	biological_process	autophagosome assembly
A	0000139	cellular_component	Golgi membrane
A	0000166	molecular_function	nucleotide binding
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	0005769	cellular_component	early endosome
A	0005783	cellular_component	endoplasmic reticulum
A	0005794	cellular_component	Golgi apparatus
A	0005829	cellular_component	cytosol
A	0006886	biological_process	intracellular protein transport
A	0006888	biological_process	endoplasmic reticulum to Golgi vesicle-mediated transport
A	0006897	biological_process	endocytosis
A	0006914	biological_process	autophagy
A	0007030	biological_process	Golgi organization
A	0012505	cellular_component	endomembrane system
A	0015031	biological_process	protein transport
A	0016020	cellular_component	membrane
A	0016192	biological_process	vesicle-mediated transport
A	0016477	biological_process	cell migration
A	0016787	molecular_function	hydrolase activity
A	0019068	biological_process	virion assembly
A	0030252	biological_process	growth hormone secretion
A	0030658	cellular_component	transport vesicle membrane
A	0032402	biological_process	melanosome transport
A	0032757	biological_process	positive regulation of interleukin-8 production
A	0034446	biological_process	substrate adhesion-dependent cell spreading
A	0042470	cellular_component	melanosome
A	0042742	biological_process	defense response to bacterium
A	0045296	molecular_function	cadherin binding
A	0046872	molecular_function	metal ion binding
A	0047496	biological_process	vesicle transport along microtubule
A	0060271	biological_process	cilium assembly
A	0070062	cellular_component	extracellular exosome
A	0090110	biological_process	COPII-coated vesicle cargo loading
A	0090557	biological_process	establishment of endothelial intestinal barrier
A	1903020	biological_process	positive regulation of glycoprotein metabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 300

Chain	Residue
A	SER25
A	THR43
A	HOH192
A	HOH194
A	GTP301

---

site_id	AC2
Number of Residues	26
Details	BINDING SITE FOR RESIDUE GTP A 301

Chain	Residue
A	LYS24
A	SER25
A	CYS26
A	TYR36
A	GLU38
A	TYR40
A	THR43
A	GLY69
A	ASN124
A	LYS125
A	ASP127
A	LEU128
A	LYS131
A	SER154
A	ALA155
A	LYS156
A	HOH192
A	HOH194
A	HOH198
A	HOH219
A	HOH244
A	MG300
A	SER20
A	GLY21
A	VAL22
A	GLY23

---

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. LLLiGDSGVGKscL

Chain	Residue	Details
A	LEU14-LEU27

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	14
Details	Motif: {"description":"Switch 1","evidences":[{"source":"PubMed","id":"22416225","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3SFV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3TKL","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	17
Details	Motif: {"description":"Switch 2","evidences":[{"source":"PubMed","id":"22416225","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3SFV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3TKL","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22416225","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3TKL","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22416225","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22939626","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23588383","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23821544","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of human RAB1A in complex with GDP.","authoringGroup":["Structural genomics consortium (SGC)"]}},{"source":"PDB","id":"2FOL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3TKL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FMB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FMC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FMD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FME","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4IRU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JVS","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22416225","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22939626","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23588383","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23821544","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of human RAB1A in complex with GDP.","authoringGroup":["Structural genomics consortium (SGC)"]}},{"source":"PDB","id":"3TKL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FMB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FMC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FMD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FME","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4IRU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JVS","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22416225","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22939626","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23588383","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of human RAB1A in complex with GDP.","authoringGroup":["Structural genomics consortium (SGC)"]}},{"source":"PDB","id":"3TKL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FMB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FMC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FMD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FME","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JVS","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"(Microbial infection) O-(2-cholinephosphoryl)serine","evidences":[{"source":"PubMed","id":"21822290","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22158903","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	Glycosylation: {"description":"(Microbial infection) N-beta-linked (GlcNAc) arginine","evidences":[{"source":"PubMed","id":"32504010","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	3
Details	Glycosylation: {"description":"(Microbial infection) N-beta-linked (GlcNAc) arginine","evidences":[{"source":"PubMed","id":"32504010","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32974215","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	3
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P51153","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---