5C2K

Crystal structure of the fusion protein linked by RhoA and the GAP domain of MgcRacGAP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000281	biological_process	mitotic cytokinesis
A	0002363	biological_process	alpha-beta T cell lineage commitment
A	0003189	biological_process	aortic valve formation
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	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005768	cellular_component	endosome
A	0005789	cellular_component	endoplasmic reticulum membrane
A	0005829	cellular_component	cytosol
A	0005856	cellular_component	cytoskeleton
A	0005886	cellular_component	plasma membrane
A	0005925	cellular_component	focal adhesion
A	0005938	cellular_component	cell cortex
A	0007165	biological_process	signal transduction
A	0007266	biological_process	Rho protein signal transduction
A	0009898	cellular_component	cytoplasmic side of plasma membrane
A	0010812	biological_process	negative regulation of cell-substrate adhesion
A	0016477	biological_process	cell migration
A	0016787	molecular_function	hydrolase activity
A	0017022	molecular_function	myosin binding
A	0019901	molecular_function	protein kinase binding
A	0021762	biological_process	substantia nigra development
A	0030027	cellular_component	lamellipodium
A	0030036	biological_process	actin cytoskeleton organization
A	0030054	cellular_component	cell junction
A	0030334	biological_process	regulation of cell migration
A	0030335	biological_process	positive regulation of cell migration
A	0030425	cellular_component	dendrite
A	0030496	cellular_component	midbody
A	0030667	cellular_component	secretory granule membrane
A	0031122	biological_process	cytoplasmic microtubule organization
A	0031982	cellular_component	vesicle
A	0032154	cellular_component	cleavage furrow
A	0032467	biological_process	positive regulation of cytokinesis
A	0032587	cellular_component	ruffle membrane
A	0032956	biological_process	regulation of actin cytoskeleton organization
A	0033688	biological_process	regulation of osteoblast proliferation
A	0034329	biological_process	cell junction assembly
A	0034446	biological_process	substrate adhesion-dependent cell spreading
A	0035385	biological_process	Roundabout signaling pathway
A	0036089	biological_process	cleavage furrow formation
A	0038027	biological_process	apolipoprotein A-I-mediated signaling pathway
A	0042476	biological_process	odontogenesis
A	0043123	biological_process	positive regulation of canonical NF-kappaB signal transduction
A	0043149	biological_process	stress fiber assembly
A	0043197	cellular_component	dendritic spine
A	0043296	cellular_component	apical junction complex
A	0043297	biological_process	apical junction assembly
A	0043366	biological_process	beta selection
A	0043542	biological_process	endothelial cell migration
A	0043931	biological_process	ossification involved in bone maturation
A	0044319	biological_process	wound healing, spreading of cells
A	0045198	biological_process	establishment of epithelial cell apical/basal polarity
A	0045666	biological_process	positive regulation of neuron differentiation
A	0045792	biological_process	negative regulation of cell size
A	0046638	biological_process	positive regulation of alpha-beta T cell differentiation
A	0050919	biological_process	negative chemotaxis
A	0051301	biological_process	cell division
A	0051496	biological_process	positive regulation of stress fiber assembly
A	0051893	biological_process	regulation of focal adhesion assembly
A	0060071	biological_process	Wnt signaling pathway, planar cell polarity pathway
A	0060193	biological_process	positive regulation of lipase activity
A	0061430	biological_process	bone trabecula morphogenesis
A	0070062	cellular_component	extracellular exosome
A	0070507	biological_process	regulation of microtubule cytoskeleton organization
A	0071222	biological_process	cellular response to lipopolysaccharide
A	0071345	biological_process	cellular response to cytokine stimulus
A	0071526	biological_process	semaphorin-plexin signaling pathway
A	0071902	biological_process	positive regulation of protein serine/threonine kinase activity
A	0071944	cellular_component	cell periphery
A	0090051	biological_process	negative regulation of cell migration involved in sprouting angiogenesis
A	0090307	biological_process	mitotic spindle assembly
A	0090324	biological_process	negative regulation of oxidative phosphorylation
A	0097498	biological_process	endothelial tube lumen extension
A	0098794	cellular_component	postsynapse
A	0098978	cellular_component	glutamatergic synapse
A	0099159	biological_process	regulation of modification of postsynaptic structure
A	0101003	cellular_component	ficolin-1-rich granule membrane
A	1901224	biological_process	positive regulation of non-canonical NF-kappaB signal transduction
A	1902766	biological_process	skeletal muscle satellite cell migration
A	1903427	biological_process	negative regulation of reactive oxygen species biosynthetic process
A	1903673	biological_process	mitotic cleavage furrow formation
A	1904996	biological_process	positive regulation of leukocyte adhesion to vascular endothelial cell
A	1905274	biological_process	regulation of modification of postsynaptic actin cytoskeleton
A	1990869	biological_process	cellular response to chemokine
A	2000406	biological_process	positive regulation of T cell migration

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue MG A 501

Chain	Residue
A	THR19
A	THR37
A	AF3502
A	GDP503
A	HOH695
A	HOH753

---

site_id	AC2
Number of Residues	13
Details	binding site for residue AF3 A 502

Chain	Residue
A	PRO36
A	THR37
A	GLY62
A	GLN63
A	ARG247
A	MG501
A	GDP503
A	HOH695
A	HOH697
A	HOH753
A	GLY14
A	ALA15
A	LYS18

---

site_id	AC3
Number of Residues	27
Details	binding site for residue GDP A 503

Chain	Residue
A	ALA15
A	CYS16
A	GLY17
A	LYS18
A	THR19
A	CYS20
A	PHE30
A	TYR34
A	LYS118
A	ASP120
A	LEU121
A	SER160
A	ALA161
A	LYS162
A	ARG247
A	MG501
A	AF3502
A	HOH639
A	HOH695
A	HOH752
A	HOH753
A	HOH773
A	HOH799
A	HOH817
A	HOH834
A	HOH869
A	HOH911

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	17
Details	Region: {"description":"Switch II region; involved in RAP1GDS1 isoform 2 binding","evidences":[{"source":"PubMed","id":"30190425","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5ZHX","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	Motif: {"description":"Effector region","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	10
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10748207","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12777804","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	13
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P62820","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"(Microbial infection) O-AMP-tyrosine; by Haemophilus IbpA; alternate","evidences":[{"source":"PubMed","id":"19362538","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"(Microbial infection) O-AMP-threonine; by Vibrio VopS","evidences":[{"source":"PubMed","id":"19039103","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"(Microbial infection) ADP-ribosylasparagine; by botulinum toxin","evidences":[{"source":"PubMed","id":"1328215","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	Modified residue: {"description":"5-glutamyl serotonin","evidences":[{"source":"UniProtKB","id":"Q9QUI0","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	Lipidation: {"description":"(Microbial infection) N6-stearoyl lysine","evidences":[{"source":"PubMed","id":"30061757","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	1
Details	Glycosylation: {"description":"(Microbial infection) O-linked (GlcNAc) tyrosine; by Photorhabdus PAU_02230; alternate","evidences":[{"source":"PubMed","id":"24141704","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	1
Details	Glycosylation: {"description":"(Microbial infection) O-linked (Glc) threonine; by C.difficile toxins TcdA and TcdB; alternate","evidences":[{"source":"PubMed","id":"24905543","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7775453","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7777059","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI12
Number of Residues	1
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"23871831","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI13
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI14
Number of Residues	190
Details	Domain: {"description":"Rho-GAP","evidences":[{"source":"PROSITE-ProRule","id":"PRU00172","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI15
Number of Residues	1
Details	Site: {"description":"Arginine finger; crucial for GTP hydrolysis by stabilizing the transition state","evidences":[{"source":"PROSITE-ProRule","id":"PRU00172","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI16
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine; by AURKB","evidences":[{"source":"PubMed","id":"12689593","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---