Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6RYU

Nucleosome-CHD4 complex structure (two CHD4 copies)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000786	cellular_component	nucleosome
A	0003677	molecular_function	DNA binding
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005694	cellular_component	chromosome
A	0030527	molecular_function	structural constituent of chromatin
A	0046982	molecular_function	protein heterodimerization activity
B	0000786	cellular_component	nucleosome
B	0003677	molecular_function	DNA binding
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005694	cellular_component	chromosome
B	0006334	biological_process	nucleosome assembly
B	0030527	molecular_function	structural constituent of chromatin
B	0046982	molecular_function	protein heterodimerization activity
C	0000786	cellular_component	nucleosome
C	0003677	molecular_function	DNA binding
C	0005634	cellular_component	nucleus
C	0005694	cellular_component	chromosome
C	0030527	molecular_function	structural constituent of chromatin
C	0046982	molecular_function	protein heterodimerization activity
D	0000786	cellular_component	nucleosome
D	0003677	molecular_function	DNA binding
D	0005515	molecular_function	protein binding
D	0005634	cellular_component	nucleus
D	0005694	cellular_component	chromosome
D	0030527	molecular_function	structural constituent of chromatin
D	0046982	molecular_function	protein heterodimerization activity
E	0000786	cellular_component	nucleosome
E	0003677	molecular_function	DNA binding
E	0005515	molecular_function	protein binding
E	0005634	cellular_component	nucleus
E	0005654	cellular_component	nucleoplasm
E	0005694	cellular_component	chromosome
E	0030527	molecular_function	structural constituent of chromatin
E	0046982	molecular_function	protein heterodimerization activity
F	0000786	cellular_component	nucleosome
F	0003677	molecular_function	DNA binding
F	0005515	molecular_function	protein binding
F	0005634	cellular_component	nucleus
F	0005694	cellular_component	chromosome
F	0006334	biological_process	nucleosome assembly
F	0030527	molecular_function	structural constituent of chromatin
F	0046982	molecular_function	protein heterodimerization activity
G	0000786	cellular_component	nucleosome
G	0003677	molecular_function	DNA binding
G	0005634	cellular_component	nucleus
G	0005694	cellular_component	chromosome
G	0030527	molecular_function	structural constituent of chromatin
G	0046982	molecular_function	protein heterodimerization activity
H	0000786	cellular_component	nucleosome
H	0003677	molecular_function	DNA binding
H	0005515	molecular_function	protein binding
H	0005634	cellular_component	nucleus
H	0005694	cellular_component	chromosome
H	0030527	molecular_function	structural constituent of chromatin
H	0046982	molecular_function	protein heterodimerization activity
V	0003677	molecular_function	DNA binding
V	0005524	molecular_function	ATP binding
V	0006338	biological_process	chromatin remodeling
V	0140658	molecular_function	ATP-dependent chromatin remodeler activity
W	0003677	molecular_function	DNA binding
W	0005524	molecular_function	ATP binding
W	0006338	biological_process	chromatin remodeling
W	0140658	molecular_function	ATP-dependent chromatin remodeler activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	binding site for residue ANP W 2201

Chain	Residue
W	HIS727
W	ARG1162
W	ILE1163
W	MG2202
W	MET753
W	GLY754
W	GLY756
W	LYS757
W	THR758
W	VAL759
W	TRP797
W	ARG1159

site_id	AC2
Number of Residues	3
Details	binding site for residue MG W 2202

Chain	Residue
W	ASP873
W	GLU874
W	ANP2201

site_id	AC3
Number of Residues	4
Details	binding site for residue ZN W 2203

Chain	Residue
W	CYS452
W	CYS455
W	HIS472
W	CYS475

site_id	AC4
Number of Residues	5
Details	binding site for residue ZN W 2204

Chain	Residue
W	CYS464
W	CYS467
W	SER469
W	CYS490
W	CYS493

site_id	AC5
Number of Residues	12
Details	binding site for residue ANP V 2201

Chain	Residue
V	HIS727
V	MET753
V	GLY754
V	GLY756
V	LYS757
V	THR758
V	VAL759
V	TRP797
V	ARG1159
V	ARG1162
V	ILE1163
V	MG2202

site_id	AC6
Number of Residues	3
Details	binding site for residue MG V 2202

Chain	Residue
V	ASP873
V	GLU874
V	ANP2201

site_id	AC7
Number of Residues	4
Details	binding site for residue ZN V 2203

Chain	Residue
V	CYS452
V	CYS455
V	HIS472
V	CYS475

site_id	AC8
Number of Residues	5
Details	binding site for residue ZN V 2204

Chain	Residue
V	CYS464
V	CYS467
V	SER469
V	CYS490
V	CYS493

Functional Information from PROSITE/UniProt

site_id	PS01359
Number of Residues	42
Details	ZF_PHD_1 Zinc finger PHD-type signature. CevCqqggei.......................................IlCdt..Cpra.YHmvCldpdmekapegk.................................WsCphC

Chain	Residue	Details
W	CYS373-CYS414
W	CYS452-CYS493

site_id	PS00357
Number of Residues	23
Details	HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG

Chain	Residue	Details
D	ARG89-GLY111

site_id	PS00047
Number of Residues	5
Details	HISTONE_H4 Histone H4 signature. GAKRH

Chain	Residue	Details
B	GLY14-HIS18

site_id	PS00598
Number of Residues	21
Details	CHROMO_1 Chromo domain signature. FfVKWqGMsywhc.SWVSelqL

Chain	Residue	Details
W	PHE543-LEU563
W	TYR640-VAL659

site_id	PS00690
Number of Residues	10
Details	DEAH_ATP_HELICASE DEAH-box subfamily ATP-dependent helicases signature. AcLIVDEAHR

Chain	Residue	Details
W	ALA868-ARG877

site_id	PS00046
Number of Residues	7
Details	HISTONE_H2A Histone H2A signature. AGLqFPV

Chain	Residue	Details
C	ALA21-VAL27

site_id	PS00959
Number of Residues	9
Details	HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI

Chain	Residue	Details
A	PRO66-ILE74

site_id	PS00322
Number of Residues	7
Details	HISTONE_H3_1 Histone H3 signature 1. KAPRKQL

Chain	Residue	Details
A	LYS14-LEU20

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	94
Details	ZN_FING: PHD-type 1 => ECO:0000255\|PROSITE-ProRule:PRU00146

Chain	Residue	Details
H	LYS2
H	LYS9
H	LYS12
H	LYS17
W	GLN370-GLU417
V	GLN370-GLU417
D	LYS12
D	LYS17

site_id	SWS_FT_FI2
Number of Residues	94
Details	ZN_FING: PHD-type 2 => ECO:0000255\|PROSITE-ProRule:PRU00146

Chain	Residue	Details
W	MET449-PRO496
V	MET449-PRO496

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU00541

Chain	Residue	Details
W	ASP751
V	ASP751
G	LYS9
G	LYS95

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:20068231, ECO:0007744\|PubMed:21406692

Chain	Residue	Details
H	LYS117
W	SER44
V	SER44

site_id	SWS_FT_FI5
Number of Residues	6
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:21406692, ECO:0007744\|PubMed:23186163

Chain	Residue	Details
F	LYS44
F	LYS79
V	SER1753
V	SER1818
W	SER303
W	SER1753
W	SER1818
V	SER303

site_id	SWS_FT_FI6
Number of Residues	8
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:21406692

Chain	Residue	Details
V	SER308
V	SER309
V	SER310
V	SER319
W	SER310
W	SER319
W	SER308
W	SER309

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0007744\|PubMed:24275569

Chain	Residue	Details
F	LYS31
F	LYS91
W	THR367
V	THR367

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:17081983, ECO:0007744\|PubMed:21406692

Chain	Residue	Details
G	LYS15
G	LYS119
C	LYS15
C	LYS119
W	SER428
V	SER428
G	LYS13

site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:18669648, ECO:0007744\|PubMed:21406692, ECO:0007744\|PubMed:24275569

Chain	Residue	Details
F	TYR51
F	TYR88
W	SER515
V	SER515

site_id	SWS_FT_FI10
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0007744\|PubMed:21406692

Chain	Residue	Details
V	THR517
A	LYS27
A	LYS36
A	LYS64
E	LYS18
E	LYS23
E	LYS27
E	LYS36
E	LYS64
W	THR517

site_id	SWS_FT_FI11
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0007744\|PubMed:18669648

Chain	Residue	Details
V	THR529
W	THR529

site_id	SWS_FT_FI12
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:18669648, ECO:0007744\|PubMed:24275569

Chain	Residue	Details
V	SER531
W	SER531

site_id	SWS_FT_FI13
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0007744\|PubMed:23186163

Chain	Residue	Details
F	LYS91
V	THR703
W	THR703

site_id	SWS_FT_FI14
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:Q6PDQ2

Chain	Residue	Details
V	SER1425
W	SER1425

site_id	SWS_FT_FI15
Number of Residues	6
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:23186163

Chain	Residue	Details
V	SER1786
V	SER1792
W	SER1792
V	SER1524
W	SER1524
W	SER1786

site_id	SWS_FT_FI16
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:17525332

Chain	Residue	Details
V	SER1565
W	SER1565

site_id	SWS_FT_FI17
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:Q12873

Chain	Residue	Details
V	SER1586
E	THR80
E	THR107
W	SER1586

site_id	SWS_FT_FI18
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:17081983, ECO:0007744\|PubMed:20068231, ECO:0007744\|PubMed:23186163

Chain	Residue	Details
W	SER1747
V	SER1747

site_id	SWS_FT_FI19
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:18669648, ECO:0007744\|PubMed:20068231, ECO:0007744\|PubMed:21406692, ECO:0007744\|PubMed:23186163, ECO:0007744\|PubMed:24275569

Chain	Residue	Details
W	SER1751
V	SER1751

site_id	SWS_FT_FI20
Number of Residues	4
Details	MOD_RES: Phosphothreonine => ECO:0000250\|UniProtKB:Q6PDQ2

Chain	Residue	Details
W	THR1758
W	THR1765
V	THR1758
V	THR1765

site_id	SWS_FT_FI21
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0007744\|PubMed:19690332, ECO:0007744\|PubMed:23186163

Chain	Residue	Details
W	THR1769
V	THR1769

site_id	SWS_FT_FI22
Number of Residues	2
Details	MOD_RES: N6-acetyllysine; alternate => ECO:0007744\|PubMed:19608861

Chain	Residue	Details
W	LYS1859
V	LYS1859

site_id	SWS_FT_FI23
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0007744\|PubMed:20068231, ECO:0007744\|PubMed:23186163, ECO:0007744\|PubMed:24275569

Chain	Residue	Details
W	THR1869
V	THR1869

site_id	SWS_FT_FI24
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0007744\|PubMed:20068231, ECO:0007744\|PubMed:23186163

Chain	Residue	Details
W	THR1895
V	THR1895

site_id	SWS_FT_FI25
Number of Residues	38
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744\|PubMed:28112733

Chain	Residue	Details
W	LYS133
W	LYS146
W	LYS179
W	LYS297
W	LYS304
W	LYS696
W	LYS1428
W	LYS1444
W	LYS1455
W	LYS1744
W	LYS1745
W	LYS1800
W	LYS1822
W	LYS1833
W	LYS1852
W	LYS1876
W	LYS1903
W	LYS2081
V	LYS133
V	LYS146
V	LYS179
V	LYS297
V	LYS304
V	LYS696
V	LYS1428
V	LYS1444
V	LYS1455
V	LYS1744
V	LYS1745
V	LYS1800
V	LYS1822
V	LYS1833
V	LYS1852
V	LYS1876
V	LYS1903
V	LYS2081

site_id	SWS_FT_FI26
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0000250\|UniProtKB:Q12873

Chain	Residue	Details
W	LYS618
V	LYS618

site_id	SWS_FT_FI27
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744\|PubMed:28112733

Chain	Residue	Details
W	LYS711
V	LYS711

site_id	SWS_FT_FI28
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744\|PubMed:25114211, ECO:0007744\|PubMed:25218447, ECO:0007744\|PubMed:25755297, ECO:0007744\|PubMed:28112733

Chain	Residue	Details
W	LYS1520
V	LYS1520

site_id	SWS_FT_FI29
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744\|PubMed:25218447, ECO:0007744\|PubMed:28112733

Chain	Residue	Details
W	LYS1781
V	LYS1781

site_id	SWS_FT_FI30
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744\|PubMed:25218447, ECO:0007744\|PubMed:25755297, ECO:0007744\|PubMed:28112733

Chain	Residue	Details
W	LYS1788
V	LYS1788

site_id	SWS_FT_FI31
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744\|PubMed:25755297, ECO:0007744\|PubMed:28112733

Chain	Residue	Details
W	LYS1859
V	LYS1859

site_id	SWS_FT_FI32
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744\|PubMed:25218447, ECO:0007744\|PubMed:25755297, ECO:0007744\|PubMed:25772364, ECO:0007744\|PubMed:28112733

Chain	Residue	Details
W	LYS1863
W	LYS1886
V	LYS1863
V	LYS1886

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