Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3R45

Structure of a CENP-A-Histone H4 Heterodimer in complex with chaperone HJURP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000132	biological_process	establishment of mitotic spindle orientation
A	0000281	biological_process	mitotic cytokinesis
A	0000775	cellular_component	chromosome, centromeric region
A	0000779	cellular_component	condensed chromosome, centromeric region
A	0000786	cellular_component	nucleosome
A	0003677	molecular_function	DNA binding
A	0003682	molecular_function	chromatin binding
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005694	cellular_component	chromosome
A	0005721	cellular_component	pericentric heterochromatin
A	0005829	cellular_component	cytosol
A	0030527	molecular_function	structural constituent of chromatin
A	0034080	biological_process	CENP-A containing chromatin assembly
A	0043505	cellular_component	CENP-A containing nucleosome
A	0046982	molecular_function	protein heterodimerization activity
A	0051301	biological_process	cell division
A	0051382	biological_process	kinetochore assembly
A	0061638	cellular_component	CENP-A containing chromatin
A	0061644	biological_process	protein localization to CENP-A containing chromatin
A	0071459	biological_process	protein localization to chromosome, centromeric region
B	0000781	cellular_component	chromosome, telomeric region
B	0000786	cellular_component	nucleosome
B	0003677	molecular_function	DNA binding
B	0003723	molecular_function	RNA 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	0006325	biological_process	chromatin organization
B	0006334	biological_process	nucleosome assembly
B	0016020	cellular_component	membrane
B	0030527	molecular_function	structural constituent of chromatin
B	0032200	biological_process	telomere organization
B	0032991	cellular_component	protein-containing complex
B	0043505	cellular_component	CENP-A containing nucleosome
B	0045653	biological_process	negative regulation of megakaryocyte differentiation
B	0046982	molecular_function	protein heterodimerization activity
B	0061644	biological_process	protein localization to CENP-A containing chromatin
B	0070062	cellular_component	extracellular exosome
C	0005634	cellular_component	nucleus
C	0042393	molecular_function	histone binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 141

Chain	Residue
A	ARG63
A	LYS64
A	HOH150
C	GLY67

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 142

Chain	Residue
A	ARG69
A	ARG72
C	LYS72
C	ARG74

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 143

Chain	Residue
A	LYS124
A	HOH153
A	ARG118

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 144

Chain	Residue
A	ARG118
A	ARG118
A	VAL119
A	VAL119
A	THR120
A	THR120

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL A 145

Chain	Residue
A	HOH155
A	HOH155
A	HOH156

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 103

Chain	Residue
A	ARG63
B	THR30
B	PRO32
B	ARG36

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 B 104

Chain	Residue
B	LYS77
B	ARG78
B	LYS79
B	THR80
C	SO485

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 105

Chain	Residue
B	LYS31
B	ARG35
B	SO4106

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 B 106

Chain	Residue
B	THR30
B	LYS31
B	PRO32
B	ARG55
B	SO4105

site_id	BC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL B 107

Chain	Residue
B	ARG39
B	ARG45

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 C 81

Chain	Residue
C	ARG23
C	ARG27
C	ARG31
C	ARG35

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 C 82

Chain	Residue
B	THR71
C	GLN42
C	PRO43
C	PHE44
C	GLU45

site_id	BC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 C 83

Chain	Residue
C	ARG64
C	ARG69
C	LEU70

site_id	BC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 C 84

Chain	Residue
C	ASP15
C	HOH95
C	HOH98

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 C 85

Chain	Residue
A	GLN87
B	LYS77
B	SO4104
C	GLU45
C	HOH87

site_id	BC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL C 86

Chain	Residue
C	ALA24
C	ARG27
C	ARG28
C	ARG31
C	ARG35
C	HOH97

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
B	GLY14-HIS18

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

Chain	Residue	Details
A	PRO66-ILE74

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	DNA_BIND:

Chain	Residue	Details
B	LYS16-LYS20

site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000269\|PubMed:17967882

Chain	Residue	Details
B	SER1

site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Symmetric dimethylarginine; by PRMT5 and PRMT7; alternate => ECO:0000250\|UniProtKB:P62806

Chain	Residue	Details
B	ARG3
A	SER19

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: N6-lactoyllysine; alternate => ECO:0000269\|PubMed:31645732

Chain	Residue	Details
B	LYS5

site_id	SWS_FT_FI5
Number of Residues	3
Details	MOD_RES: N6-propionyllysine; alternate => ECO:0000269\|PubMed:17267393

Chain	Residue	Details
B	LYS8
B	LYS16
B	LYS44

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000269\|PubMed:22389435

Chain	Residue	Details
B	LYS12
B	LYS31
B	LYS77
B	LYS91

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: N6-methyllysine; alternate => ECO:0000269\|PubMed:12086618, ECO:0000269\|PubMed:15964846, ECO:0000269\|PubMed:17967882, ECO:0000269\|PubMed:27338793

Chain	Residue	Details
B	LYS20

site_id	SWS_FT_FI8
Number of Residues	1
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
B	SER47

site_id	SWS_FT_FI9
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0007744\|PubMed:15592455, ECO:0007744\|PubMed:20068231

Chain	Residue	Details
B	TYR51

site_id	SWS_FT_FI10
Number of Residues	1
Details	MOD_RES: N6-glutaryllysine; alternate => ECO:0000269\|PubMed:31542297

Chain	Residue	Details
B	LYS59

site_id	SWS_FT_FI11
Number of Residues	1
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250\|UniProtKB:P62806

Chain	Residue	Details
B	LYS79

site_id	SWS_FT_FI12
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0000250\|UniProtKB:P62806

Chain	Residue	Details
B	THR80

site_id	SWS_FT_FI13
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0007744\|PubMed:24275569

Chain	Residue	Details
B	TYR88

site_id	SWS_FT_FI14
Number of Residues	1
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744\|PubMed:25218447

Chain	Residue	Details
B	LYS12

site_id	SWS_FT_FI15
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269\|PubMed:19818714

Chain	Residue	Details
B	LYS91

site_id	SWS_FT_FI16
Number of Residues	3
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744\|PubMed:28112733

Chain	Residue	Details
B	LYS20
B	LYS59
B	LYS79

site_id	SWS_FT_FI17
Number of Residues	1
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate => ECO:0000269\|PubMed:30886146

Chain	Residue	Details
B	LYS31

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