2Q21

CRYSTAL STRUCTURES AT 2.2 ANGSTROMS RESOLUTION OF THE CATALYTIC DOMAINS OF NORMAL RAS PROTEIN AND AN ONCOGENIC MUTANT COMPLEXED WITH GSP

Replaces:  3P21

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000139	cellular_component	Golgi membrane
A	0000165	biological_process	MAPK cascade
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	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005789	cellular_component	endoplasmic reticulum membrane
A	0005794	cellular_component	Golgi apparatus
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0006357	biological_process	regulation of transcription by RNA polymerase II
A	0006935	biological_process	chemotaxis
A	0007165	biological_process	signal transduction
A	0007166	biological_process	cell surface receptor signaling pathway
A	0007265	biological_process	Ras protein signal transduction
A	0008284	biological_process	positive regulation of cell population proliferation
A	0008285	biological_process	negative regulation of cell population proliferation
A	0008286	biological_process	insulin receptor signaling pathway
A	0009887	biological_process	animal organ morphogenesis
A	0010629	biological_process	negative regulation of gene expression
A	0014044	biological_process	Schwann cell development
A	0016020	cellular_component	membrane
A	0016787	molecular_function	hydrolase activity
A	0019003	molecular_function	GDP binding
A	0030335	biological_process	positive regulation of cell migration
A	0032956	biological_process	regulation of actin cytoskeleton organization
A	0042127	biological_process	regulation of cell population proliferation
A	0042552	biological_process	myelination
A	0043410	biological_process	positive regulation of MAPK cascade
A	0043495	molecular_function	protein-membrane adaptor activity
A	0045944	biological_process	positive regulation of transcription by RNA polymerase II
A	0046330	biological_process	positive regulation of JNK cascade
A	0046579	biological_process	positive regulation of Ras protein signal transduction
A	0048471	cellular_component	perinuclear region of cytoplasm
A	0050679	biological_process	positive regulation of epithelial cell proliferation
A	0051726	biological_process	regulation of cell cycle
A	0060612	biological_process	adipose tissue development
A	0070374	biological_process	positive regulation of ERK1 and ERK2 cascade
A	0071480	biological_process	cellular response to gamma radiation
A	0090303	biological_process	positive regulation of wound healing
A	0090314	biological_process	positive regulation of protein targeting to membrane
A	0090398	biological_process	cellular senescence
A	0098696	biological_process	regulation of neurotransmitter receptor localization to postsynaptic specialization membrane
A	0098978	cellular_component	glutamatergic synapse
A	0160185	molecular_function	phospholipase C activator activity
A	1900029	biological_process	positive regulation of ruffle assembly
A	2000630	biological_process	positive regulation of miRNA metabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 173

Chain	Residue
A	SER17
A	GDP180
A	HOH201
A	HOH202
A	HOH203
A	HOH204

---

site_id	AC2
Number of Residues	22
Details	BINDING SITE FOR RESIDUE GDP A 180

Chain	Residue
A	GLY15
A	LYS16
A	SER17
A	ALA18
A	PHE28
A	VAL29
A	ASP30
A	ASN116
A	LYS117
A	ASP119
A	LEU120
A	SER145
A	ALA146
A	LYS147
A	MG173
A	HOH201
A	HOH202
A	HOH203
A	HOH232
A	VAL12
A	GLY13
A	VAL14

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Motif: {"description":"Effector region"}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	17
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16698776","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35522713","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Modified residue: {"description":"N-acetylmethionine; in GTPase HRas; alternate","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2008","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Calvo F.","Kolch W."]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"N-acetylthreonine; in GTPase HRas, N-terminally processed","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2008","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Calvo F.","Kolch W."]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"PubMed","id":"9020151","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Glycosylation: {"description":"(Microbial infection) O-linked (Glc) threonine; by P.sordellii toxin TcsL","evidences":[{"source":"PubMed","id":"19744486","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8626575","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8626586","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9632667","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"30442762","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1ksj

Chain	Residue	Details
A	GLN61

---