Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4S3O

PCGF5-RING1B-UbcH5c complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000122	biological_process	negative regulation of transcription by RNA polymerase II
A	0000166	molecular_function	nucleotide binding
A	0000209	biological_process	protein polyubiquitination
A	0004842	molecular_function	ubiquitin-protein transferase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0006281	biological_process	DNA repair
A	0006511	biological_process	ubiquitin-dependent protein catabolic process
A	0006513	biological_process	protein monoubiquitination
A	0006915	biological_process	apoptotic process
A	0006974	biological_process	DNA damage response
A	0010008	cellular_component	endosome membrane
A	0016567	biological_process	protein ubiquitination
A	0016740	molecular_function	transferase activity
A	0030514	biological_process	negative regulation of BMP signaling pathway
A	0036211	biological_process	protein modification process
A	0043161	biological_process	proteasome-mediated ubiquitin-dependent protein catabolic process
A	0051865	biological_process	protein autoubiquitination
A	0061630	molecular_function	ubiquitin protein ligase activity
A	0061631	molecular_function	ubiquitin conjugating enzyme activity
A	0070062	cellular_component	extracellular exosome
A	0070936	biological_process	protein K48-linked ubiquitination
A	0070979	biological_process	protein K11-linked ubiquitination
A	0085020	biological_process	protein K6-linked ubiquitination
A	1903955	biological_process	obsolete positive regulation of protein targeting to mitochondrion
B	0000151	cellular_component	ubiquitin ligase complex
D	0000122	biological_process	negative regulation of transcription by RNA polymerase II
D	0000166	molecular_function	nucleotide binding
D	0000209	biological_process	protein polyubiquitination
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	0005829	cellular_component	cytosol
D	0005886	cellular_component	plasma membrane
D	0006281	biological_process	DNA repair
D	0006511	biological_process	ubiquitin-dependent protein catabolic process
D	0006513	biological_process	protein monoubiquitination
D	0006915	biological_process	apoptotic process
D	0006974	biological_process	DNA damage response
D	0010008	cellular_component	endosome membrane
D	0016567	biological_process	protein ubiquitination
D	0016740	molecular_function	transferase activity
D	0030514	biological_process	negative regulation of BMP signaling pathway
D	0036211	biological_process	protein modification process
D	0043161	biological_process	proteasome-mediated ubiquitin-dependent protein catabolic process
D	0051865	biological_process	protein autoubiquitination
D	0061630	molecular_function	ubiquitin protein ligase activity
D	0061631	molecular_function	ubiquitin conjugating enzyme activity
D	0070062	cellular_component	extracellular exosome
D	0070936	biological_process	protein K48-linked ubiquitination
D	0070979	biological_process	protein K11-linked ubiquitination
D	0085020	biological_process	protein K6-linked ubiquitination
D	1903955	biological_process	obsolete positive regulation of protein targeting to mitochondrion
E	0000151	cellular_component	ubiquitin ligase complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 200

Chain	Residue
B	CYS51
B	CYS54
B	CYS72
B	CYS75

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 201

Chain	Residue
B	CYS67
B	HIS69
B	CYS87
B	CYS90

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN E 201

Chain	Residue
E	CYS54
E	CYS72
E	CYS75
E	CYS51

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN E 202

Chain	Residue
E	CYS67
E	HIS69
E	CYS87
E	CYS90

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 201

Chain	Residue
C	CYS18
C	CYS21
C	CYS39
C	CYS42

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 202

Chain	Residue
C	CYS34
C	HIS36
C	CYS53
C	CYS56

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN F 201

Chain	Residue
F	CYS18
F	CYS21
F	CYS39
F	CYS42

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN F 202

Chain	Residue
F	CYS34
F	HIS36
F	CYS53
F	CYS56

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	TYR74-LEU89

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

Chain	Residue	Details
C	CYS34-ILE43
B	CYS67-ILE76

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
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_FI2
Number of Residues	10
Details	Region: {"description":"Interaction with nucleosomes via an acidic patch on histone H2A and histone H2B","evidences":[{"source":"PubMed","id":"25355358","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"25519132","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"Q9CQJ4","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	40
Details	Zinc finger: {"description":"RING-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00175","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	78
Details	Zinc finger: {"description":"RING-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00175","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26151332","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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