Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6H7X

First X-ray structure of full-length human RuvB-Like 2.

Replaces: 5N7R

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000492	biological_process	box C/D snoRNP assembly
A	0000723	biological_process	telomere maintenance
A	0000786	cellular_component	nucleosome
A	0000791	cellular_component	euchromatin
A	0000812	cellular_component	Swr1 complex
A	0000978	molecular_function	RNA polymerase II cis-regulatory region sequence-specific DNA binding
A	0000979	molecular_function	RNA polymerase II core promoter sequence-specific DNA binding
A	0001094	molecular_function	TFIID-class transcription factor complex binding
A	0003678	molecular_function	DNA helicase activity
A	0003714	molecular_function	transcription corepressor activity
A	0004386	molecular_function	helicase 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	0005813	cellular_component	centrosome
A	0005829	cellular_component	cytosol
A	0006275	biological_process	regulation of DNA replication
A	0006281	biological_process	DNA repair
A	0006282	biological_process	regulation of DNA repair
A	0006310	biological_process	DNA recombination
A	0006325	biological_process	chromatin organization
A	0006338	biological_process	chromatin remodeling
A	0006355	biological_process	regulation of DNA-templated transcription
A	0006357	biological_process	regulation of transcription by RNA polymerase II
A	0006457	biological_process	protein folding
A	0008013	molecular_function	beta-catenin binding
A	0008094	molecular_function	ATP-dependent activity, acting on DNA
A	0016020	cellular_component	membrane
A	0016363	cellular_component	nuclear matrix
A	0016787	molecular_function	hydrolase activity
A	0016887	molecular_function	ATP hydrolysis activity
A	0017025	molecular_function	TBP-class protein binding
A	0031011	cellular_component	Ino80 complex
A	0031490	molecular_function	chromatin DNA binding
A	0032508	biological_process	DNA duplex unwinding
A	0033044	biological_process	regulation of chromosome organization
A	0034644	biological_process	cellular response to UV
A	0035267	cellular_component	NuA4 histone acetyltransferase complex
A	0042802	molecular_function	identical protein binding
A	0042803	molecular_function	protein homodimerization activity
A	0042981	biological_process	regulation of apoptotic process
A	0043531	molecular_function	ADP binding
A	0045739	biological_process	positive regulation of DNA repair
A	0045892	biological_process	negative regulation of DNA-templated transcription
A	0045893	biological_process	positive regulation of DNA-templated transcription
A	0045944	biological_process	positive regulation of transcription by RNA polymerase II
A	0045995	biological_process	regulation of embryonic development
A	0050821	biological_process	protein stabilization
A	0051082	molecular_function	unfolded protein binding
A	0051117	molecular_function	ATPase binding
A	0051276	biological_process	chromosome organization
A	0051726	biological_process	regulation of cell cycle
A	0060382	biological_process	regulation of DNA strand elongation
A	0070062	cellular_component	extracellular exosome
A	0071169	biological_process	establishment of protein localization to chromatin
A	0071339	cellular_component	MLL1 complex
A	0071392	biological_process	cellular response to estradiol stimulus
A	0090090	biological_process	negative regulation of canonical Wnt signaling pathway
A	0097255	cellular_component	R2TP complex
A	0101031	cellular_component	protein folding chaperone complex
A	0120293	cellular_component	dynein axonemal particle
A	0140585	molecular_function	promoter-enhancer loop anchoring activity
A	1904507	biological_process	positive regulation of telomere maintenance in response to DNA damage
A	1904874	biological_process	positive regulation of telomerase RNA localization to Cajal body
A	1905168	biological_process	positive regulation of double-strand break repair via homologous recombination
A	1990062	cellular_component	RPAP3/R2TP/prefoldin-like complex
A	1990904	cellular_component	ribonucleoprotein complex
A	2000779	biological_process	regulation of double-strand break repair

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	binding site for residue MG A 1001

Chain	Residue
A	ASP305
A	ARG336
A	PEG1005

site_id	AC2
Number of Residues	2
Details	binding site for residue MG A 1002

Chain	Residue
A	SER398
A	GLU436

site_id	AC3
Number of Residues	1
Details	binding site for residue MG A 1003

Chain	Residue
A	ASP366

site_id	AC4
Number of Residues	4
Details	binding site for residue EDO A 1004

Chain	Residue
A	LEU432
A	VAL357
A	SER358
A	SER431

site_id	AC5
Number of Residues	5
Details	binding site for residue PEG A 1005

Chain	Residue
A	ASP305
A	ILE306
A	GLU307
A	GLY337
A	MG1001

site_id	AC6
Number of Residues	5
Details	binding site for residue EDO A 1006

Chain	Residue
A	LYS83
A	ASP299
A	GLU300
A	THR328
A	ASN329

site_id	AC7
Number of Residues	4
Details	binding site for residue EDO A 1007

Chain	Residue
A	THR440
A	GLN441
A	TYR442
A	MET443

site_id	AC8
Number of Residues	2
Details	binding site for residue EDO A 1008

Chain	Residue
A	GLN92
A	EDO1009

site_id	AC9
Number of Residues	1
Details	binding site for residue EDO A 1009

Chain	Residue
A	EDO1008

site_id	AD1
Number of Residues	5
Details	binding site for residue EDO A 1010

Chain	Residue
A	GLY80
A	THR81
A	GLY82
A	LYS83
A	THR84

site_id	AD2
Number of Residues	2
Details	binding site for residue EDO A 1011

Chain	Residue
A	GLU381
A	ARG414

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	BINDING:

Chain	Residue	Details
A	GLY77

site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: N-acetylalanine => ECO:0000269\|Ref.14, ECO:0007744\|PubMed:19413330, ECO:0007744\|PubMed:22814378, ECO:0007744\|PubMed:25944712

Chain	Residue	Details
A	ALA2

site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:23186163

Chain	Residue	Details
A	SER437

site_id	SWS_FT_FI4
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744\|PubMed:28112733

Chain	Residue	Details
A	LYS9
A	LYS444
A	LYS456

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