Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3PTF

X-ray structure of the non-covalent complex between UbcH5A and Ubiquitin

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	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006511	biological_process	ubiquitin-dependent protein catabolic process
A	0016567	biological_process	protein ubiquitination
A	0016740	molecular_function	transferase activity
A	0030514	biological_process	negative regulation of BMP signaling pathway
A	0031398	biological_process	positive regulation of protein ubiquitination
A	0031669	biological_process	cellular response to nutrient levels
A	0032991	cellular_component	protein-containing complex
A	0038202	biological_process	TORC1 signaling
A	0043161	biological_process	proteasome-mediated ubiquitin-dependent protein catabolic process
A	0061630	molecular_function	ubiquitin protein ligase activity
A	0061631	molecular_function	ubiquitin conjugating enzyme activity
A	0070936	biological_process	protein K48-linked ubiquitination
A	1902916	biological_process	positive regulation of protein polyubiquitination
A	1904262	biological_process	negative regulation of TORC1 signaling
B	0000122	biological_process	negative regulation of transcription by RNA polymerase II
B	0000166	molecular_function	nucleotide binding
B	0000209	biological_process	protein polyubiquitination
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	0006511	biological_process	ubiquitin-dependent protein catabolic process
B	0016567	biological_process	protein ubiquitination
B	0016740	molecular_function	transferase activity
B	0030514	biological_process	negative regulation of BMP signaling pathway
B	0031398	biological_process	positive regulation of protein ubiquitination
B	0031669	biological_process	cellular response to nutrient levels
B	0032991	cellular_component	protein-containing complex
B	0038202	biological_process	TORC1 signaling
B	0043161	biological_process	proteasome-mediated ubiquitin-dependent protein catabolic process
B	0061630	molecular_function	ubiquitin protein ligase activity
B	0061631	molecular_function	ubiquitin conjugating enzyme activity
B	0070936	biological_process	protein K48-linked ubiquitination
B	1902916	biological_process	positive regulation of protein polyubiquitination
B	1904262	biological_process	negative regulation of TORC1 signaling

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

Chain	Residue	Details
C	LYS27-ASP52

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	SITE: Interacts with activating enzyme

Chain	Residue	Details
C	ARG54
C	ARG72
D	ARG54
D	ARG72

site_id	SWS_FT_FI2
Number of Residues	2
Details	SITE: Essential for function

Chain	Residue	Details
C	HIS68
D	HIS68

site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphoserine; by PINK1 => ECO:0000269\|PubMed:24660806, ECO:0000269\|PubMed:24751536, ECO:0000269\|PubMed:24784582, ECO:0000269\|PubMed:25527291

Chain	Residue	Details
C	SER65
D	SER65

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: (Microbial infection) ADP-ribosylthreonine => ECO:0000269\|PubMed:32330457

Chain	Residue	Details
C	THR66
D	THR66

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: ADP-ribosylglycine => ECO:0000269\|PubMed:28525742

Chain	Residue	Details
C	GLY76
D	GLY76

site_id	SWS_FT_FI6
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269\|PubMed:16443603

Chain	Residue	Details
C	LYS6
D	LYS6

site_id	SWS_FT_FI7
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)

Chain	Residue	Details
C	GLY76
D	GLY76

site_id	SWS_FT_FI8
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269\|PubMed:16443603, ECO:0000269\|PubMed:16543144

Chain	Residue	Details
C	LYS11
C	LYS48
D	LYS11
D	LYS48

site_id	SWS_FT_FI9
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305\|PubMed:15466860

Chain	Residue	Details
C	LYS27
D	LYS27

site_id	SWS_FT_FI10
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269\|PubMed:16543144, ECO:0000269\|PubMed:25752573, ECO:0000269\|PubMed:25752577, ECO:0000269\|PubMed:34239127

Chain	Residue	Details
C	LYS29
D	LYS29

site_id	SWS_FT_FI11
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269\|PubMed:25752577

Chain	Residue	Details
C	LYS33
D	LYS33

site_id	SWS_FT_FI12
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269\|PubMed:16543144, ECO:0000269\|PubMed:18719106

Chain	Residue	Details
C	LYS63
D	LYS63

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