Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3HCU

Crystal structure of TRAF6 in complex with Ubc13 in the C2 space group

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004842	molecular_function	ubiquitin-protein transferase activity
A	0005164	molecular_function	tumor necrosis factor receptor binding
A	0016567	biological_process	protein ubiquitination
B	0000151	cellular_component	ubiquitin ligase complex
B	0000166	molecular_function	nucleotide binding
B	0000209	biological_process	protein polyubiquitination
B	0000724	biological_process	double-strand break repair via homologous recombination
B	0000729	biological_process	DNA double-strand break processing
B	0001650	cellular_component	fibrillar center
B	0003723	molecular_function	RNA binding
B	0004842	molecular_function	ubiquitin-protein transferase activity
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005634	cellular_component	nucleus
B	0005654	cellular_component	nucleoplasm
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006281	biological_process	DNA repair
B	0006282	biological_process	regulation of DNA repair
B	0006301	biological_process	DNA damage tolerance
B	0006513	biological_process	protein monoubiquitination
B	0006974	biological_process	DNA damage response
B	0016567	biological_process	protein ubiquitination
B	0016740	molecular_function	transferase activity
B	0031371	cellular_component	ubiquitin conjugating enzyme complex
B	0031372	cellular_component	UBC13-MMS2 complex
B	0031625	molecular_function	ubiquitin protein ligase binding
B	0032991	cellular_component	protein-containing complex
B	0043123	biological_process	positive regulation of canonical NF-kappaB signal transduction
B	0043130	molecular_function	ubiquitin binding
B	0043161	biological_process	proteasome-mediated ubiquitin-dependent protein catabolic process
B	0045739	biological_process	positive regulation of DNA repair
B	0050852	biological_process	T cell receptor signaling pathway
B	0061631	molecular_function	ubiquitin conjugating enzyme activity
B	0070062	cellular_component	extracellular exosome
B	0070534	biological_process	protein K63-linked ubiquitination
B	0097027	molecular_function	ubiquitin-protein transferase activator activity
B	0140374	biological_process	antiviral innate immune response
B	1902523	biological_process	positive regulation of protein K63-linked ubiquitination
B	1902533	biological_process	positive regulation of intracellular signal transduction
B	1904262	biological_process	negative regulation of TORC1 signaling
B	2000781	biological_process	positive regulation of double-strand break repair
C	0004842	molecular_function	ubiquitin-protein transferase activity
C	0005164	molecular_function	tumor necrosis factor receptor binding
C	0016567	biological_process	protein ubiquitination
D	0000151	cellular_component	ubiquitin ligase complex
D	0000166	molecular_function	nucleotide binding
D	0000209	biological_process	protein polyubiquitination
D	0000724	biological_process	double-strand break repair via homologous recombination
D	0000729	biological_process	DNA double-strand break processing
D	0001650	cellular_component	fibrillar center
D	0003723	molecular_function	RNA binding
D	0004842	molecular_function	ubiquitin-protein transferase activity
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005634	cellular_component	nucleus
D	0005654	cellular_component	nucleoplasm
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006281	biological_process	DNA repair
D	0006282	biological_process	regulation of DNA repair
D	0006301	biological_process	DNA damage tolerance
D	0006513	biological_process	protein monoubiquitination
D	0006974	biological_process	DNA damage response
D	0016567	biological_process	protein ubiquitination
D	0016740	molecular_function	transferase activity
D	0031371	cellular_component	ubiquitin conjugating enzyme complex
D	0031372	cellular_component	UBC13-MMS2 complex
D	0031625	molecular_function	ubiquitin protein ligase binding
D	0032991	cellular_component	protein-containing complex
D	0043123	biological_process	positive regulation of canonical NF-kappaB signal transduction
D	0043130	molecular_function	ubiquitin binding
D	0043161	biological_process	proteasome-mediated ubiquitin-dependent protein catabolic process
D	0045739	biological_process	positive regulation of DNA repair
D	0050852	biological_process	T cell receptor signaling pathway
D	0061631	molecular_function	ubiquitin conjugating enzyme activity
D	0070062	cellular_component	extracellular exosome
D	0070534	biological_process	protein K63-linked ubiquitination
D	0097027	molecular_function	ubiquitin-protein transferase activator activity
D	0140374	biological_process	antiviral innate immune response
D	1902523	biological_process	positive regulation of protein K63-linked ubiquitination
D	1902533	biological_process	positive regulation of intracellular signal transduction
D	1904262	biological_process	negative regulation of TORC1 signaling
D	2000781	biological_process	positive regulation of double-strand break repair

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 301

Chain	Residue
A	CYS70
A	CYS73
A	CYS90
A	CYS93

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 302

Chain	Residue
A	CYS85
A	HIS87
A	CYS105
A	ASP108

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 303

Chain	Residue
A	CYS139
A	HIS151
A	CYS155
A	CYS134

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN C 304

Chain	Residue
C	GLY55
C	CYS70
C	CYS73
C	CYS90
C	CYS93

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 305

Chain	Residue
C	CYS85
C	HIS87
C	CYS105
C	ASP108

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN C 306

Chain	Residue
C	CYS134
C	CYS139
C	CYS155

Functional Information from PROSITE/UniProt

site_id	PS00183
Number of Residues	16
Details	UBC_1 Ubiquitin-conjugating (UBC) active site signature. YHPNVdkl.GrICLdiL

Chain	Residue	Details
B	TYR76-LEU91

site_id	PS00518
Number of Residues	10
Details	ZF_RING_1 Zinc finger RING-type signature. CgHrFCkaCI

Chain	Residue	Details
A	CYS85-ILE94

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	78
Details	Zinc finger: {"description":"RING-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00175","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"PubMed","id":"17135271","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19825828","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)","evidences":[{"source":"PubMed","id":"18093978","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	292
Details	Domain: {"description":"UBC core","evidences":[{"source":"PROSITE-ProRule","id":"PRU00388","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Active site: {"description":"Glycyl thioester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00388","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)","evidences":[{"source":"PubMed","id":"16112642","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16122702","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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