Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5TTE

Crystal Structure of an RBR E3 ubiquitin ligase in complex with an E2-Ub thioester intermediate mimic

Functional Information from GO Data

Chain	GOid	namespace	contents
B	0000151	cellular_component	ubiquitin ligase complex
B	0000209	biological_process	protein polyubiquitination
B	0004842	molecular_function	ubiquitin-protein transferase activity
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005654	cellular_component	nucleoplasm
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006511	biological_process	ubiquitin-dependent protein catabolic process
B	0008270	molecular_function	zinc ion binding
B	0015030	cellular_component	Cajal body
B	0016567	biological_process	protein ubiquitination
B	0016604	cellular_component	nuclear body
B	0016740	molecular_function	transferase activity
B	0019005	cellular_component	SCF ubiquitin ligase complex
B	0019787	molecular_function	ubiquitin-like protein transferase activity
B	0031462	cellular_component	Cul2-RING ubiquitin ligase complex
B	0031463	cellular_component	Cul3-RING ubiquitin ligase complex
B	0031464	cellular_component	Cul4A-RING E3 ubiquitin ligase complex
B	0031624	molecular_function	ubiquitin conjugating enzyme binding
B	0031625	molecular_function	ubiquitin protein ligase binding
B	0039585	biological_process	PKR/eIFalpha signaling
B	0046872	molecular_function	metal ion binding
B	0061630	molecular_function	ubiquitin protein ligase activity
B	0097413	cellular_component	Lewy body
E	0000151	cellular_component	ubiquitin ligase complex
E	0000209	biological_process	protein polyubiquitination
E	0003713	molecular_function	transcription coactivator activity
E	0003723	molecular_function	RNA binding
E	0004842	molecular_function	ubiquitin-protein transferase activity
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0005634	cellular_component	nucleus
E	0005654	cellular_component	nucleoplasm
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0006355	biological_process	regulation of DNA-templated transcription
E	0006511	biological_process	ubiquitin-dependent protein catabolic process
E	0008283	biological_process	cell population proliferation
E	0016567	biological_process	protein ubiquitination
E	0016740	molecular_function	transferase activity
E	0019787	molecular_function	ubiquitin-like protein transferase activity
E	0019899	molecular_function	enzyme binding
E	0031398	biological_process	positive regulation of protein ubiquitination
E	0031625	molecular_function	ubiquitin protein ligase binding
E	0032446	biological_process	protein modification by small protein conjugation
E	0036211	biological_process	protein modification process
E	0044770	biological_process	cell cycle phase transition
E	0045893	biological_process	positive regulation of DNA-templated transcription
E	0051443	biological_process	positive regulation of ubiquitin-protein transferase activity
E	0061631	molecular_function	ubiquitin conjugating enzyme activity
E	0070979	biological_process	protein K11-linked ubiquitination
E	0071383	biological_process	cellular response to steroid hormone stimulus
E	0071385	biological_process	cellular response to glucocorticoid stimulus
E	0097027	molecular_function	ubiquitin-protein transferase activator activity
E	0098793	cellular_component	presynapse
E	1903955	biological_process	positive regulation of protein targeting to mitochondrion
F	0003729	molecular_function	mRNA binding
F	0005634	cellular_component	nucleus
F	0005737	cellular_component	cytoplasm

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue ZN B 601

Chain	Residue
B	CYS344
B	CYS347
B	CYS362
B	CYS367

site_id	AC2
Number of Residues	4
Details	binding site for residue ZN B 602

Chain	Residue
B	CYS372
B	CYS375
B	HIS382
B	CYS389

site_id	AC3
Number of Residues	4
Details	binding site for residue ZN B 603

Chain	Residue
B	CYS189
B	CYS208
B	CYS211
B	CYS186

site_id	AC4
Number of Residues	4
Details	binding site for residue ZN B 604

Chain	Residue
B	CYS203
B	HIS205
B	CYS231
B	CYS236

site_id	AC5
Number of Residues	5
Details	binding site for residue ZN B 605

Chain	Residue
B	CYS276
B	ALA278
B	CYS281
B	CYS297
B	CYS299

site_id	AC6
Number of Residues	4
Details	binding site for residue ZN B 606

Chain	Residue
B	CYS304
B	CYS307
B	HIS312
B	CYS317

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250

Chain	Residue	Details
F	ARG48

site_id	SWS_FT_FI2
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) => ECO:0000255\|PROSITE-ProRule:PRU00214

Chain	Residue	Details
E	LYS131
F	GLY76

site_id	SWS_FT_FI3
Number of Residues	31
Details	ZN_FING: RING-type 2; atypical => ECO:0000255\|PROSITE-ProRule:PRU01221

Chain	Residue	Details
B	CYS344-CYS375

site_id	SWS_FT_FI4
Number of Residues	1
Details	ACT_SITE: ACT_SITE => ECO:0000255\|PROSITE-ProRule:PRU01221, ECO:0000269\|PubMed:21532592, ECO:0000269\|PubMed:23707686

Chain	Residue	Details
B	CYS357

site_id	SWS_FT_FI5
Number of Residues	16
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU01221, ECO:0000269\|PubMed:23707686, ECO:0007744\|PDB:4KBL, ECO:0007744\|PDB:4KC9

Chain	Residue	Details
B	CYS186
B	CYS281
B	CYS297
B	CYS299
B	CYS304
B	CYS307
B	HIS312
B	CYS317
B	CYS189
B	CYS203
B	HIS205
B	CYS208
B	CYS211
B	CYS231
B	CYS236
B	CYS276

site_id	SWS_FT_FI6
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU01221, ECO:0000269\|PubMed:15236971, ECO:0000269\|PubMed:23707686, ECO:0000269\|PubMed:24058416, ECO:0007744\|PDB:1WD2, ECO:0007744\|PDB:2M9Y, ECO:0007744\|PDB:4KBL, ECO:0007744\|PDB:4KC9

Chain	Residue	Details
B	CYS344
B	CYS347
B	CYS362
B	CYS367

site_id	SWS_FT_FI7
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU01221, ECO:0000269\|PubMed:23707686, ECO:0000269\|PubMed:24058416, ECO:0007744\|PDB:2M9Y, ECO:0007744\|PDB:4KBL, ECO:0007744\|PDB:4KC9

Chain	Residue	Details
B	CYS372
B	CYS375
B	HIS382
B	CYS389

site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: N6-acetyllysine => ECO:0000250\|UniProtKB:Q9Z1K5

Chain	Residue	Details
B	LYS142

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	1
Details	M-CSA 438

Chain	Residue	Details
E	LYS86	nucleofuge

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)