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	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	0000166	molecular_function	nucleotide binding
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	0006351	biological_process	DNA-templated transcription
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	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	1903955	biological_process	obsolete 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	50
Details	Zinc finger: {"description":"RING-type 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01221","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	61
Details	Zinc finger: {"description":"IBR-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU01221","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	31
Details	Zinc finger: {"description":"RING-type 2; atypical","evidences":[{"source":"PROSITE-ProRule","id":"PRU01221","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	48
Details	Region: {"description":"UBA-like","evidences":[{"source":"PubMed","id":"23707686","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	211
Details	Region: {"description":"TRIAD supradomain","evidences":[{"source":"PROSITE-ProRule","id":"PRU01221","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	1
Details	Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21532592","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23707686","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23707686","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4KBL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KC9","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15236971","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23707686","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24058416","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1WD2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2M9Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KBL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KC9","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23707686","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24058416","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2M9Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KBL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KC9","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9Z1K5","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	1
Details	Active site: {"description":"Glycyl thioester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00388","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10133","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	75
Details	Domain: {"description":"Ubiquitin-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00214","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	1
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)","evidences":[{"source":"PROSITE-ProRule","id":"PRU00214","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	1
Details	M-CSA 438

Chain	Residue	Details
B	GLY85	nucleofuge

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