3X1W

Ras-related protein Rap1B with GDP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003924	molecular_function	GTPase activity
A	0003925	molecular_function	G protein activity
A	0005525	molecular_function	GTP binding
A	0005811	cellular_component	lipid droplet
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0005911	cellular_component	cell-cell junction
A	0007165	biological_process	signal transduction
A	0007189	biological_process	adenylate cyclase-activating G protein-coupled receptor signaling pathway
A	0007264	biological_process	small GTPase-mediated signal transduction
A	0008283	biological_process	cell population proliferation
A	0009743	biological_process	response to carbohydrate
A	0016020	cellular_component	membrane
A	0016787	molecular_function	hydrolase activity
A	0019003	molecular_function	GDP binding
A	0030073	biological_process	insulin secretion
A	0031045	cellular_component	dense core granule
A	0032486	biological_process	Rap protein signal transduction
A	0033625	biological_process	positive regulation of integrin activation
A	0044877	molecular_function	protein-containing complex binding
A	0045121	cellular_component	membrane raft
A	0045955	biological_process	negative regulation of calcium ion-dependent exocytosis
A	0061028	biological_process	establishment of endothelial barrier
A	0070161	cellular_component	anchoring junction
A	0070374	biological_process	positive regulation of ERK1 and ERK2 cascade
A	0071320	biological_process	cellular response to cAMP
A	0097211	biological_process	cellular response to gonadotropin-releasing hormone
A	0098978	cellular_component	glutamatergic synapse
A	0099010	biological_process	modification of postsynaptic structure
A	1901888	biological_process	regulation of cell junction assembly
A	1904322	biological_process	cellular response to forskolin
A	2000114	biological_process	regulation of establishment of cell polarity
A	2000301	biological_process	negative regulation of synaptic vesicle exocytosis

Functional Information from PDB Data

site_id	AC1
Number of Residues	24
Details	BINDING SITE FOR RESIDUE GDP A 201

Chain	Residue
A	GLY13
A	GLU45
A	ASN116
A	LYS117
A	ASP119
A	LEU120
A	SER147
A	ALA148
A	LYS149
A	MG202
A	HOH301
A	VAL14
A	HOH303
A	HOH304
A	HOH309
A	HOH324
A	HOH353
A	GLY15
A	LYS16
A	SER17
A	ALA18
A	PHE28
A	GLU30
A	LYS31

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 202

Chain	Residue
A	SER17
A	GDP201
A	HOH301
A	HOH302
A	HOH303
A	HOH304

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CD A 203

Chain	Residue
A	ASP122
A	GLU156
A	ASP160
A	ARG163
A	HOH337
A	HOH350

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	42
Details	Region: {"description":"Interaction with KRIT1","evidences":[{"source":"UniProtKB","id":"P61224","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	8
Details	Motif: {"description":"Effector region","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	17
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P61224","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"ADP-ribosylserine; by botulinum toxin","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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