3DPL

Structural Insights into NEDD8 Activation of Cullin-RING Ligases: Conformational Control of Conjugation.

Functional Information from GO Data

Chain	GOid	namespace	contents
C	0006511	biological_process	ubiquitin-dependent protein catabolic process
C	0031461	cellular_component	cullin-RING ubiquitin ligase complex
C	0031625	molecular_function	ubiquitin protein ligase binding
R	0000165	biological_process	MAPK cascade
R	0000209	biological_process	protein polyubiquitination
R	0004842	molecular_function	ubiquitin-protein transferase activity
R	0005515	molecular_function	protein binding
R	0005634	cellular_component	nucleus
R	0005654	cellular_component	nucleoplasm
R	0005737	cellular_component	cytoplasm
R	0005829	cellular_component	cytosol
R	0006281	biological_process	DNA repair
R	0006511	biological_process	ubiquitin-dependent protein catabolic process
R	0006513	biological_process	protein monoubiquitination
R	0006974	biological_process	DNA damage response
R	0007283	biological_process	spermatogenesis
R	0008270	molecular_function	zinc ion binding
R	0016567	biological_process	protein ubiquitination
R	0016740	molecular_function	transferase activity
R	0019005	cellular_component	SCF ubiquitin ligase complex
R	0019788	molecular_function	NEDD8 transferase activity
R	0030163	biological_process	protein catabolic process
R	0031146	biological_process	SCF-dependent proteasomal ubiquitin-dependent protein catabolic process
R	0031461	cellular_component	cullin-RING ubiquitin ligase complex
R	0031462	cellular_component	Cul2-RING ubiquitin ligase complex
R	0031463	cellular_component	Cul3-RING ubiquitin ligase complex
R	0031464	cellular_component	Cul4A-RING E3 ubiquitin ligase complex
R	0031465	cellular_component	Cul4B-RING E3 ubiquitin ligase complex
R	0031466	cellular_component	Cul5-RING ubiquitin ligase complex
R	0031467	cellular_component	Cul7-RING ubiquitin ligase complex
R	0031625	molecular_function	ubiquitin protein ligase binding
R	0032436	biological_process	positive regulation of proteasomal ubiquitin-dependent protein catabolic process
R	0032480	biological_process	negative regulation of type I interferon production
R	0034450	molecular_function	ubiquitin-ubiquitin ligase activity
R	0034644	biological_process	cellular response to UV
R	0042110	biological_process	T cell activation
R	0043123	biological_process	positive regulation of canonical NF-kappaB signal transduction
R	0043161	biological_process	proteasome-mediated ubiquitin-dependent protein catabolic process
R	0043687	biological_process	post-translational protein modification
R	0045116	biological_process	protein neddylation
R	0045732	biological_process	positive regulation of protein catabolic process
R	0046872	molecular_function	metal ion binding
R	0060090	molecular_function	molecular adaptor activity
R	0061629	molecular_function	RNA polymerase II-specific DNA-binding transcription factor binding
R	0061630	molecular_function	ubiquitin protein ligase activity
R	0061663	molecular_function	NEDD8 ligase activity
R	0062197	biological_process	cellular response to chemical stress
R	0070936	biological_process	protein K48-linked ubiquitination
R	0071230	biological_process	cellular response to amino acid stimulus
R	0090090	biological_process	negative regulation of canonical Wnt signaling pathway
R	0097602	molecular_function	cullin family protein binding
R	0140627	biological_process	ubiquitin-dependent protein catabolic process via the C-end degron rule pathway
R	1902499	biological_process	positive regulation of protein autoubiquitination
R	1902883	biological_process	negative regulation of response to oxidative stress
R	1904263	biological_process	positive regulation of TORC1 signaling

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN R 201

Chain	Residue
R	CYS42
R	CYS45
R	HIS80
R	CYS83

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site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN R 202

Chain	Residue
R	CYS75
R	HIS77
R	CYS94
R	ASP97

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site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN R 203

Chain	Residue
R	CYS56
R	CYS68
R	HIS82
R	CYS53

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Functional Information from PROSITE/UniProt

site_id	PS01256
Number of Residues	28
Details	CULLIN_1 Cullin family signature. IKeqIewLIEHkYIrRdesdintFiYmA

Chain	Residue	Details
C	ILE753-ALA780

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	45
Details	ZN_FING: RING-type => ECO:0000255|PROSITE-ProRule:PRU00175

Chain	Residue	Details
R	CYS53-ASN98

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site_id	SWS_FT_FI2
Number of Residues	11
Details	BINDING: BINDING => ECO:0000269|PubMed:11961546, ECO:0007744|PDB:1LDJ, ECO:0007744|PDB:1LDK, ECO:0007744|PDB:1U6G, ECO:0007744|PDB:2HYE, ECO:0007744|PDB:3DPL, ECO:0007744|PDB:3DQV, ECO:0007744|PDB:3RTR, ECO:0007744|PDB:4F52, ECO:0007744|PDB:4P5O

Chain	Residue	Details
R	CYS42
R	CYS94
R	ASP97
R	CYS45
R	CYS53
R	CYS56
R	CYS68
R	CYS75
R	HIS77
R	HIS80
R	HIS82

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site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:11961546, ECO:0007744|PDB:1LDJ, ECO:0007744|PDB:1LDK, ECO:0007744|PDB:1U6G, ECO:0007744|PDB:2HYE, ECO:0007744|PDB:3DQV, ECO:0007744|PDB:3RTR, ECO:0007744|PDB:4F52, ECO:0007744|PDB:4P5O

Chain	Residue	Details
R	CYS83

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163

Chain	Residue	Details
R	THR9

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