4DXA

Co-crystal structure of Rap1 in complex with KRIT1

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	0005515	molecular_function	protein binding
A	0005525	molecular_function	GTP binding
A	0005737	cellular_component	cytoplasm
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	0007264	biological_process	small GTPase-mediated signal transduction
A	0008283	biological_process	cell population proliferation
A	0016020	cellular_component	membrane
A	0016787	molecular_function	hydrolase activity
A	0017156	biological_process	calcium-ion regulated exocytosis
A	0019003	molecular_function	GDP binding
A	0032486	biological_process	Rap protein signal transduction
A	0033625	biological_process	positive regulation of integrin activation
A	0035577	cellular_component	azurophil granule membrane
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	0051649	biological_process	establishment of localization in cell
A	0061028	biological_process	establishment of endothelial barrier
A	0070062	cellular_component	extracellular exosome
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	0098978	cellular_component	glutamatergic synapse
A	0099010	biological_process	modification of postsynaptic structure
A	1901888	biological_process	regulation of cell junction assembly
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	26
Details	BINDING SITE FOR RESIDUE GSP A 201

Chain	Residue
A	VAL12
A	GLU30
A	TYR32
A	THR35
A	GLY60
A	ASN116
A	LYS117
A	ASP119
A	LEU120
A	SER147
A	ALA148
A	GLY13
A	LYS149
A	MG202
A	HOH316
A	HOH354
A	HOH374
A	HOH382
A	HOH386
A	VAL14
A	GLY15
A	LYS16
A	SER17
A	ALA18
A	PHE28
A	VAL29

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 202

Chain	Residue
A	SER17
A	THR35
A	GSP201
A	HOH381
A	HOH382

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	42
Details	Region: {"description":"Interaction with KRIT1","evidences":[{"source":"PubMed","id":"22577140","evidenceCode":"ECO:0000269"}]}

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":"PubMed","id":"18309292","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22577140","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"ADP-ribosylserine; by botulinum toxin","evidences":[{"source":"PubMed","id":"3141412","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	22
Details	Region: {"description":"Interaction with RAP1B","evidences":[{"source":"PubMed","id":"22577140","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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