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	0005737	cellular_component	cytoplasm
A	0005768	cellular_component	endosome
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

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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

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269|PubMed:22416225, ECO:0007744|PDB:3TKL

Chain	Residue	Details
A	SER20
A	ASP127
A	ALA155
A	LYS156
A	GLY21
A	GLY23
A	LYS24
A	CYS26
A	GLU38
A	GLY69
A	ASN124
A	LYS125

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:22416225, ECO:0000269|PubMed:22939626, ECO:0000269|PubMed:23588383, ECO:0000269|PubMed:23821544, ECO:0000269|Ref.29, ECO:0007744|PDB:2FOL, ECO:0007744|PDB:3TKL, ECO:0007744|PDB:4FMB, ECO:0007744|PDB:4FMC, ECO:0007744|PDB:4FMD, ECO:0007744|PDB:4FME, ECO:0007744|PDB:4IRU, ECO:0007744|PDB:4JVS

Chain	Residue	Details
A	SER25

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:22416225, ECO:0000269|PubMed:22939626, ECO:0000269|PubMed:23588383, ECO:0000269|PubMed:23821544, ECO:0000269|Ref.29, ECO:0007744|PDB:3TKL, ECO:0007744|PDB:4FMB, ECO:0007744|PDB:4FMC, ECO:0007744|PDB:4FMD, ECO:0007744|PDB:4FME, ECO:0007744|PDB:4IRU, ECO:0007744|PDB:4JVS

Chain	Residue	Details
A	THR43

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:22416225, ECO:0000269|PubMed:22939626, ECO:0000269|PubMed:23588383, ECO:0000269|Ref.29, ECO:0007744|PDB:3TKL, ECO:0007744|PDB:4FMB, ECO:0007744|PDB:4FMC, ECO:0007744|PDB:4FMD, ECO:0007744|PDB:4FME, ECO:0007744|PDB:4JVS

Chain	Residue	Details
A	ASP66

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: N-acetylserine => ECO:0000269|Ref.9, ECO:0007744|PubMed:22223895

Chain	Residue	Details
A	SER2

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: (Microbial infection) O-(2-cholinephosphoryl)serine => ECO:0000269|PubMed:21822290, ECO:0000269|PubMed:22158903

Chain	Residue	Details
A	SER79

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	CARBOHYD: (Microbial infection) N-beta-linked (GlcNAc) arginine => ECO:0000269|PubMed:32504010

Chain	Residue	Details
A	ARG72

---

site_id	SWS_FT_FI8
Number of Residues	3
Details	CARBOHYD: (Microbial infection) N-beta-linked (GlcNAc) arginine => ECO:0000269|PubMed:32504010, ECO:0000269|PubMed:32974215

Chain	Residue	Details
A	ARG74
A	ARG82
A	ARG111

---

site_id	SWS_FT_FI9
Number of Residues	3
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P51153

Chain	Residue	Details
A	LYS49
A	LYS61

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