Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6PAI

Structure of the human DDB1-DDA1-DCAF15 E3 ubiquitin ligase bound to RBM39 and sulfonamide E7820

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000781	cellular_component	chromosome, telomeric region
A	0003676	molecular_function	nucleic acid binding
A	0003677	molecular_function	DNA binding
A	0003684	molecular_function	damaged DNA binding
A	0005515	molecular_function	protein binding
A	0005615	cellular_component	extracellular space
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005730	cellular_component	nucleolus
A	0005737	cellular_component	cytoplasm
A	0006281	biological_process	DNA repair
A	0006289	biological_process	nucleotide-excision repair
A	0006511	biological_process	ubiquitin-dependent protein catabolic process
A	0006915	biological_process	apoptotic process
A	0006974	biological_process	DNA damage response
A	0007056	biological_process	spindle assembly involved in female meiosis
A	0010498	biological_process	proteasomal protein catabolic process
A	0016055	biological_process	Wnt signaling pathway
A	0016567	biological_process	protein ubiquitination
A	0019076	biological_process	viral release from host cell
A	0030674	molecular_function	protein-macromolecule adaptor activity
A	0031464	cellular_component	Cul4A-RING E3 ubiquitin ligase complex
A	0031465	cellular_component	Cul4B-RING E3 ubiquitin ligase complex
A	0032991	cellular_component	protein-containing complex
A	0034644	biological_process	cellular response to UV
A	0035234	biological_process	ectopic germ cell programmed cell death
A	0035861	cellular_component	site of double-strand break
A	0042752	biological_process	regulation of circadian rhythm
A	0043066	biological_process	negative regulation of apoptotic process
A	0043161	biological_process	proteasome-mediated ubiquitin-dependent protein catabolic process
A	0044725	biological_process	epigenetic programming in the zygotic pronuclei
A	0044877	molecular_function	protein-containing complex binding
A	0045070	biological_process	positive regulation of viral genome replication
A	0045722	biological_process	positive regulation of gluconeogenesis
A	0045732	biological_process	positive regulation of protein catabolic process
A	0046726	biological_process	positive regulation by virus of viral protein levels in host cell
A	0048511	biological_process	rhythmic process
A	0051093	biological_process	negative regulation of developmental process
A	0051702	biological_process	biological process involved in interaction with symbiont
A	0070062	cellular_component	extracellular exosome
A	0070914	biological_process	UV-damage excision repair
A	0071987	molecular_function	WD40-repeat domain binding
A	0080008	cellular_component	Cul4-RING E3 ubiquitin ligase complex
A	0097602	molecular_function	cullin family protein binding
A	0160072	molecular_function	ubiquitin ligase complex scaffold activity
A	1901990	biological_process	regulation of mitotic cell cycle phase transition
A	2000242	biological_process	negative regulation of reproductive process
C	0016567	biological_process	protein ubiquitination
D	0003676	molecular_function	nucleic acid binding
D	0003723	molecular_function	RNA binding
D	0005634	cellular_component	nucleus
D	0006397	biological_process	mRNA processing
E	0000209	biological_process	protein polyubiquitination
E	0005515	molecular_function	protein binding
E	0005654	cellular_component	nucleoplasm
E	0016567	biological_process	protein ubiquitination
E	0032434	biological_process	regulation of proteasomal ubiquitin-dependent protein catabolic process
E	0032436	biological_process	positive regulation of proteasomal ubiquitin-dependent protein catabolic process
E	0080008	cellular_component	Cul4-RING E3 ubiquitin ligase complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	binding site for residue EPE A 1301

Chain	Residue
A	GLY17
A	CYS18
A	GLU65
A	HIS261
A	ASN262
A	ARG263
A	TYR271
A	EPE1302

site_id	AC2
Number of Residues	5
Details	binding site for residue EPE A 1302

Chain	Residue
A	HIS261
A	GLU312
A	ARG327
A	EPE1301
A	CYS260

site_id	AC3
Number of Residues	13
Details	binding site for residue O6M C 901

Chain	Residue
C	THR230
C	PHE231
C	GLN232
C	PRO233
C	ALA234
C	PHE235
C	VAL477
C	ARG552
C	CYS555
C	VAL556
C	LEU563
D	ASP264
D	MET265

site_id	AC4
Number of Residues	4
Details	binding site for residue ZN C 902

Chain	Residue
C	CYS193
C	CYS196
C	CYS211
C	HIS214

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744\|PubMed:28112733

Chain	Residue	Details
D	LYS244
C	CYS196
C	CYS211
C	HIS214

site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:20068231, ECO:0007744\|PubMed:23186163, ECO:0007744\|PubMed:24275569

Chain	Residue	Details
E	SER33

site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:18669648, ECO:0007744\|PubMed:20068231, ECO:0007744\|PubMed:21406692, ECO:0007744\|PubMed:24275569

Chain	Residue	Details
E	SER95

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:23186163

Chain	Residue	Details
C	SER50
C	VAL418

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:18669648

Chain	Residue	Details
C	LEU422

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