9L6F

Crystal structure of KRas G12D (GDP) in complex with ASP3082

This is a non-PDB format compatible entry.

Functional Information from GO Data

Chain	GOid	namespace	contents
C	0000151	cellular_component	ubiquitin ligase complex
C	0001222	molecular_function	transcription corepressor binding
C	0005515	molecular_function	protein binding
C	0005634	cellular_component	nucleus
C	0005654	cellular_component	nucleoplasm
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006367	biological_process	transcription initiation at RNA polymerase II promoter
C	0006368	biological_process	transcription elongation by RNA polymerase II
C	0016567	biological_process	protein ubiquitination
C	0030891	cellular_component	VCB complex
C	0031462	cellular_component	Cul2-RING ubiquitin ligase complex
C	0031466	cellular_component	Cul5-RING ubiquitin ligase complex
C	0031625	molecular_function	ubiquitin protein ligase binding
C	0032436	biological_process	positive regulation of proteasomal ubiquitin-dependent protein catabolic process
C	0065003	biological_process	protein-containing complex assembly
C	0070449	cellular_component	elongin complex
C	0140627	biological_process	ubiquitin-dependent protein catabolic process via the C-end degron rule pathway
C	0140958	biological_process	target-directed miRNA degradation
G	0000151	cellular_component	ubiquitin ligase complex
G	0001222	molecular_function	transcription corepressor binding
G	0005515	molecular_function	protein binding
G	0005634	cellular_component	nucleus
G	0005654	cellular_component	nucleoplasm
G	0005737	cellular_component	cytoplasm
G	0005829	cellular_component	cytosol
G	0006367	biological_process	transcription initiation at RNA polymerase II promoter
G	0006368	biological_process	transcription elongation by RNA polymerase II
G	0016567	biological_process	protein ubiquitination
G	0030891	cellular_component	VCB complex
G	0031462	cellular_component	Cul2-RING ubiquitin ligase complex
G	0031466	cellular_component	Cul5-RING ubiquitin ligase complex
G	0031625	molecular_function	ubiquitin protein ligase binding
G	0032436	biological_process	positive regulation of proteasomal ubiquitin-dependent protein catabolic process
G	0065003	biological_process	protein-containing complex assembly
G	0070449	cellular_component	elongin complex
G	0140627	biological_process	ubiquitin-dependent protein catabolic process via the C-end degron rule pathway
G	0140958	biological_process	target-directed miRNA degradation
K	0000151	cellular_component	ubiquitin ligase complex
K	0001222	molecular_function	transcription corepressor binding
K	0005515	molecular_function	protein binding
K	0005634	cellular_component	nucleus
K	0005654	cellular_component	nucleoplasm
K	0005737	cellular_component	cytoplasm
K	0005829	cellular_component	cytosol
K	0006367	biological_process	transcription initiation at RNA polymerase II promoter
K	0006368	biological_process	transcription elongation by RNA polymerase II
K	0016567	biological_process	protein ubiquitination
K	0030891	cellular_component	VCB complex
K	0031462	cellular_component	Cul2-RING ubiquitin ligase complex
K	0031466	cellular_component	Cul5-RING ubiquitin ligase complex
K	0031625	molecular_function	ubiquitin protein ligase binding
K	0032436	biological_process	positive regulation of proteasomal ubiquitin-dependent protein catabolic process
K	0065003	biological_process	protein-containing complex assembly
K	0070449	cellular_component	elongin complex
K	0140627	biological_process	ubiquitin-dependent protein catabolic process via the C-end degron rule pathway
K	0140958	biological_process	target-directed miRNA degradation
O	0000151	cellular_component	ubiquitin ligase complex
O	0001222	molecular_function	transcription corepressor binding
O	0005515	molecular_function	protein binding
O	0005634	cellular_component	nucleus
O	0005654	cellular_component	nucleoplasm
O	0005737	cellular_component	cytoplasm
O	0005829	cellular_component	cytosol
O	0006367	biological_process	transcription initiation at RNA polymerase II promoter
O	0006368	biological_process	transcription elongation by RNA polymerase II
O	0016567	biological_process	protein ubiquitination
O	0030891	cellular_component	VCB complex
O	0031462	cellular_component	Cul2-RING ubiquitin ligase complex
O	0031466	cellular_component	Cul5-RING ubiquitin ligase complex
O	0031625	molecular_function	ubiquitin protein ligase binding
O	0032436	biological_process	positive regulation of proteasomal ubiquitin-dependent protein catabolic process
O	0065003	biological_process	protein-containing complex assembly
O	0070449	cellular_component	elongin complex
O	0140627	biological_process	ubiquitin-dependent protein catabolic process via the C-end degron rule pathway
O	0140958	biological_process	target-directed miRNA degradation

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	220
Details	Region: {"description":"Involved in binding to CCT complex"}

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Residue

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site_id	SWS_FT_FI2
Number of Residues	36
Details	Region: {"description":"Interaction with Elongin BC complex"}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	4
Details	Modified residue: {"description":"N-acetylmethionine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2009","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Waridel P.","Quadroni M."]}},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}

Chain

Residue

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site_id	SWS_FT_FI4
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P62869","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI5
Number of Residues	130
Details	Domain: {"description":"Ubiquitin-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00214","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	32
Details	Motif: {"description":"Effector region"}

Chain

Residue

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site_id	SWS_FT_FI7
Number of Residues	72
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22431598","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22566140","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"34380736","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"35522713","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI8
Number of Residues	4
Details	Modified residue: {"description":"N-acetylthreonine; in GTPase KRas, 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

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site_id	SWS_FT_FI9
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"22711838","evidenceCode":"ECO:0000269"}]}

Chain

Residue

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site_id	SWS_FT_FI10
Number of Residues	4
Details	Glycosylation: {"description":"(Microbial infection) O-linked (Glc) threonine; by P.sordellii toxin TcsL","evidences":[{"source":"PubMed","id":"19744486","evidenceCode":"ECO:0000269"}]}

Chain

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