Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4H9S

Complex structure 6 of DAXX/H3.3(sub7)/H4

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000775	cellular_component	chromosome, centromeric region
A	0000781	cellular_component	chromosome, telomeric region
A	0000785	cellular_component	chromatin
A	0000786	cellular_component	nucleosome
A	0000939	cellular_component	inner kinetochore
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	0001556	biological_process	oocyte maturation
A	0001649	biological_process	osteoblast differentiation
A	0001740	cellular_component	Barr body
A	0003677	molecular_function	DNA binding
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005694	cellular_component	chromosome
A	0006334	biological_process	nucleosome assembly
A	0006997	biological_process	nucleus organization
A	0007283	biological_process	spermatogenesis
A	0007286	biological_process	spermatid development
A	0007338	biological_process	single fertilization
A	0007566	biological_process	embryo implantation
A	0008283	biological_process	cell population proliferation
A	0008584	biological_process	male gonad development
A	0030307	biological_process	positive regulation of cell growth
A	0030527	molecular_function	structural constituent of chromatin
A	0031492	molecular_function	nucleosomal DNA binding
A	0031508	biological_process	pericentric heterochromatin formation
A	0031509	biological_process	subtelomeric heterochromatin formation
A	0032200	biological_process	telomere organization
A	0032991	cellular_component	protein-containing complex
A	0035264	biological_process	multicellular organism growth
A	0042692	biological_process	muscle cell differentiation
A	0043229	cellular_component	intracellular organelle
A	0046982	molecular_function	protein heterodimerization activity
A	0048477	biological_process	oogenesis
A	0070062	cellular_component	extracellular exosome
A	0090230	biological_process	regulation of centromere complex assembly
A	1902340	biological_process	negative regulation of chromosome condensation
B	0000775	cellular_component	chromosome, centromeric region
B	0000781	cellular_component	chromosome, telomeric region
B	0000785	cellular_component	chromatin
B	0000786	cellular_component	nucleosome
B	0000939	cellular_component	inner kinetochore
B	0000978	molecular_function	RNA polymerase II cis-regulatory region sequence-specific DNA binding
B	0000979	molecular_function	RNA polymerase II core promoter sequence-specific DNA binding
B	0001556	biological_process	oocyte maturation
B	0001649	biological_process	osteoblast differentiation
B	0001740	cellular_component	Barr body
B	0003677	molecular_function	DNA binding
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005634	cellular_component	nucleus
B	0005654	cellular_component	nucleoplasm
B	0005694	cellular_component	chromosome
B	0006334	biological_process	nucleosome assembly
B	0006997	biological_process	nucleus organization
B	0007283	biological_process	spermatogenesis
B	0007286	biological_process	spermatid development
B	0007338	biological_process	single fertilization
B	0007566	biological_process	embryo implantation
B	0008283	biological_process	cell population proliferation
B	0008584	biological_process	male gonad development
B	0030307	biological_process	positive regulation of cell growth
B	0030527	molecular_function	structural constituent of chromatin
B	0031492	molecular_function	nucleosomal DNA binding
B	0031508	biological_process	pericentric heterochromatin formation
B	0031509	biological_process	subtelomeric heterochromatin formation
B	0032200	biological_process	telomere organization
B	0032991	cellular_component	protein-containing complex
B	0035264	biological_process	multicellular organism growth
B	0042692	biological_process	muscle cell differentiation
B	0043229	cellular_component	intracellular organelle
B	0046982	molecular_function	protein heterodimerization activity
B	0048477	biological_process	oogenesis
B	0070062	cellular_component	extracellular exosome
B	0090230	biological_process	regulation of centromere complex assembly
B	1902340	biological_process	negative regulation of chromosome condensation
C	0003677	molecular_function	DNA binding
C	0030527	molecular_function	structural constituent of chromatin
C	0046982	molecular_function	protein heterodimerization activity
D	0003677	molecular_function	DNA binding
D	0030527	molecular_function	structural constituent of chromatin
D	0046982	molecular_function	protein heterodimerization activity
E	0042393	molecular_function	histone binding
F	0042393	molecular_function	histone binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 C 201

Chain	Residue
A	ILE62
A	ARG63
C	ILE29
C	THR30
C	ALA33

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 D 201

Chain	Residue
D	THR30
D	ALA33
B	ILE62
B	ARG63
D	GLY28
D	ILE29

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PO4 E 401

Chain	Residue
A	ALA47
A	LEU48
A	ARG49
E	THR262
E	ARG263
E	TYR264
E	MET312
E	HOH522

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 F 401

Chain	Residue
B	ALA47
B	LEU48
F	THR262
F	ARG263
F	TYR264

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PO4 F 402

Chain	Residue
A	ARG52
F	GLY250
F	ARG251
F	VAL252
F	ASP331
F	TYR334
F	ASN335
F	HOH527

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LYS14-LEU20

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

Chain	Residue	Details
A	PRO66-ILE74

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:18669648

Chain	Residue	Details
E	SER213
F	SER213

site_id	SWS_FT_FI2
Number of Residues	6
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000269\|PubMed:22389435

Chain	Residue	Details
C	LYS31
C	LYS77
C	LYS91
D	LYS31
D	LYS77
D	LYS91

site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: N6-propionyllysine; alternate => ECO:0000269\|PubMed:17267393

Chain	Residue	Details
C	LYS44
D	LYS44

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphoserine; by PAK2 => ECO:0000269\|PubMed:21724829, ECO:0007744\|PubMed:17081983, ECO:0007744\|PubMed:18669648, ECO:0007744\|PubMed:19690332, ECO:0007744\|PubMed:20068231, ECO:0007744\|PubMed:21406692, ECO:0007744\|PubMed:23186163, ECO:0007744\|PubMed:24275569

Chain	Residue	Details
C	SER47
D	SER47

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphotyrosine => ECO:0007744\|PubMed:15592455, ECO:0007744\|PubMed:20068231

Chain	Residue	Details
C	TYR51
D	TYR51

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: N6-glutaryllysine; alternate => ECO:0000269\|PubMed:31542297

Chain	Residue	Details
C	LYS59
D	LYS59

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250\|UniProtKB:P62806

Chain	Residue	Details
C	LYS79
D	LYS79

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0000250\|UniProtKB:P62806

Chain	Residue	Details
C	THR80
D	THR80

site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: Phosphotyrosine => ECO:0007744\|PubMed:24275569

Chain	Residue	Details
C	TYR88
D	TYR88

site_id	SWS_FT_FI10
Number of Residues	6
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744\|PubMed:28112733

Chain	Residue	Details
C	LYS20
C	LYS59
C	LYS79
D	LYS20
D	LYS59
D	LYS79

site_id	SWS_FT_FI11
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269\|PubMed:19818714

Chain	Residue	Details
A	LYS14
C	LYS91
B	LYS14
D	LYS91

site_id	SWS_FT_FI12
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate => ECO:0000269\|PubMed:30886146

Chain	Residue	Details
C	LYS31
D	LYS31

site_id	SWS_FT_FI13
Number of Residues	4
Details	MOD_RES: N6-methyllysine; alternate => ECO:0000269\|PubMed:16267050, ECO:0000269\|PubMed:17194708

Chain	Residue	Details
A	LYS18
A	LYS64
B	LYS18
B	LYS64

site_id	SWS_FT_FI14
Number of Residues	2
Details	MOD_RES: N6-methyllysine; alternate => ECO:0000269\|PubMed:17194708

Chain	Residue	Details
A	LYS23
B	LYS23

site_id	SWS_FT_FI15
Number of Residues	2
Details	MOD_RES: Citrulline => ECO:0000269\|PubMed:16567635

Chain	Residue	Details
A	ARG26
B	ARG26

site_id	SWS_FT_FI16
Number of Residues	4
Details	MOD_RES: N6-methyllysine; alternate => ECO:0000269\|PubMed:16185088, ECO:0000269\|PubMed:16267050, ECO:0000269\|PubMed:17194708, ECO:0000269\|PubMed:7309716

Chain	Residue	Details
A	LYS27
A	LYS36
B	LYS27
B	LYS36

site_id	SWS_FT_FI17
Number of Residues	2
Details	MOD_RES: Phosphoserine; alternate; by AURKB, AURKC and RPS6KA5 => ECO:0000269\|PubMed:10464286, ECO:0000269\|PubMed:11856369, ECO:0000269\|PubMed:15681610, ECO:0000269\|PubMed:15684425, ECO:0000269\|PubMed:15851689, ECO:0000269\|PubMed:16185088

Chain	Residue	Details
A	SER28
B	SER28

site_id	SWS_FT_FI18
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000269\|PubMed:15851689, ECO:0000269\|PubMed:16185088

Chain	Residue	Details
A	SER31
B	SER31

site_id	SWS_FT_FI19
Number of Residues	2
Details	MOD_RES: N6-methyllysine => ECO:0000250\|UniProtKB:P68431

Chain	Residue	Details
A	LYS37
B	LYS37

site_id	SWS_FT_FI20
Number of Residues	2
Details	MOD_RES: Phosphotyrosine => ECO:0000269\|PubMed:19783980

Chain	Residue	Details
A	TYR41
B	TYR41

site_id	SWS_FT_FI21
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000269\|PubMed:20850016

Chain	Residue	Details
A	SER57
B	SER57

site_id	SWS_FT_FI22
Number of Residues	2
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000269\|PubMed:22389435, ECO:0000269\|PubMed:29211711

Chain	Residue	Details
A	LYS79
B	LYS79

site_id	SWS_FT_FI23
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0000269\|PubMed:20850016

Chain	Residue	Details
A	THR80
B	THR80

site_id	SWS_FT_FI24
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:24275569

Chain	Residue	Details
A	SER86
B	SER86

site_id	SWS_FT_FI25
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0000250\|UniProtKB:Q71DI3

Chain	Residue	Details
A	THR107
B	THR107

site_id	SWS_FT_FI26
Number of Residues	2
Details	MOD_RES: N6-glutaryllysine; alternate => ECO:0000269\|PubMed:31542297

Chain	Residue	Details
A	LYS115
B	LYS115

site_id	SWS_FT_FI27
Number of Residues	2
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000269\|PubMed:22389435, ECO:0000269\|PubMed:27436229

Chain	Residue	Details
A	LYS122
B	LYS122

site_id	SWS_FT_FI28
Number of Residues	2
Details	LIPID: N6-decanoyllysine => ECO:0000269\|PubMed:35939806

Chain	Residue	Details
A	LYS18
B	LYS18

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