Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6N13

UbcH7-Ub Complex with R0RBR Parkin and phosphoubiquitin

Functional Information from GO Data

Chain	GOid	namespace	contents
B	0004842	molecular_function	ubiquitin-protein transferase activity
B	0005739	cellular_component	mitochondrion
B	0005829	cellular_component	cytosol
B	0008270	molecular_function	zinc ion binding
B	0016567	biological_process	protein ubiquitination
C	0000151	cellular_component	ubiquitin ligase complex
C	0000166	molecular_function	nucleotide binding
C	0000209	biological_process	protein polyubiquitination
C	0003713	molecular_function	transcription coactivator activity
C	0003723	molecular_function	RNA binding
C	0004842	molecular_function	ubiquitin-protein transferase activity
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005634	cellular_component	nucleus
C	0005654	cellular_component	nucleoplasm
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006351	biological_process	DNA-templated transcription
C	0006355	biological_process	regulation of DNA-templated transcription
C	0006511	biological_process	ubiquitin-dependent protein catabolic process
C	0008283	biological_process	cell population proliferation
C	0016567	biological_process	protein ubiquitination
C	0016740	molecular_function	transferase activity
C	0019787	molecular_function	ubiquitin-like protein transferase activity
C	0019899	molecular_function	enzyme binding
C	0031398	biological_process	positive regulation of protein ubiquitination
C	0031625	molecular_function	ubiquitin protein ligase binding
C	0032446	biological_process	protein modification by small protein conjugation
C	0036211	biological_process	protein modification process
C	0044770	biological_process	cell cycle phase transition
C	0045893	biological_process	positive regulation of DNA-templated transcription
C	0061631	molecular_function	ubiquitin conjugating enzyme activity
C	0070979	biological_process	protein K11-linked ubiquitination
C	0071383	biological_process	cellular response to steroid hormone stimulus
C	0071385	biological_process	cellular response to glucocorticoid stimulus
C	0097027	molecular_function	ubiquitin-protein transferase activator activity
C	1903955	biological_process	obsolete positive regulation of protein targeting to mitochondrion

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue ZN B 501

Chain	Residue
B	CYS253
B	HIS257
B	CYS289
B	CYS293

site_id	AC2
Number of Residues	3
Details	binding site for residue ZN B 502

Chain	Residue
B	GLU370
B	HIS373
B	CYS377

site_id	AC3
Number of Residues	2
Details	binding site for residue ZN B 503

Chain	Residue
B	CYS449
B	CYS457

site_id	AC4
Number of Residues	4
Details	binding site for residue ZN B 504

Chain	Residue
B	CYS166
B	CYS169
B	CYS196
B	CYS201

site_id	AC5
Number of Residues	4
Details	binding site for residue ZN B 505

Chain	Residue
B	CYS238
B	CYS241
B	CYS260
B	CYS263

site_id	AC6
Number of Residues	5
Details	binding site for residue ZN B 506

Chain	Residue
B	CYS337
B	CYS352
B	LEU358
B	GLY359
B	CYS360

site_id	AC7
Number of Residues	4
Details	binding site for residue ZN B 507

Chain	Residue
B	CYS418
B	ARG420
B	CYS421
B	CYS436

site_id	AC8
Number of Residues	4
Details	binding site for residue ZN B 508

Chain	Residue
B	CYS150
B	CYS154
B	CYS212
B	HIS215

Functional Information from PROSITE/UniProt

site_id	PS00299
Number of Residues	26
Details	UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD

Chain	Residue	Details
A	LYS27-ASP52
D	LYS727-ASP752

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	55
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	64
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	34
Details	Region: {"description":"SYT11 binding 1","evidences":[{"source":"PubMed","id":"12925569","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	231
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	36
Details	Region: {"description":"SYT11 binding 2","evidences":[{"source":"PubMed","id":"12925569","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	32
Details	Region: {"description":"REP","evidences":[{"source":"UniProtKB","id":"Q9JK66","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	1
Details	Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23770917","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01221","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23770917","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine; by PINK1","evidences":[{"source":"PubMed","id":"18957282","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18957282","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	3
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)","evidences":[{"source":"PubMed","id":"27534820","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	75
Details	Domain: {"description":"Ubiquitin-like 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00214","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	147
Details	Domain: {"description":"UBC core","evidences":[{"source":"PROSITE-ProRule","id":"PRU00388","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
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_FI17
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	1
Details	M-CSA 438

Chain	Residue	Details
C	LYS586	nucleofuge

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)