6AE8

Structure insight into histone chaperone Chz1-mediated H2A.Z recognition and replacement

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000786	cellular_component	nucleosome
A	0003677	molecular_function	DNA binding
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	0030527	molecular_function	structural constituent of chromatin
B	0046982	molecular_function	protein heterodimerization activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	binding site for residue BCN A 201

Chain	Residue
A	ARG1
A	LYS2
A	TYR5
A	ASN35
A	PHE38
A	GLU39
A	ARG117

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site_id	AC2
Number of Residues	9
Details	binding site for residue BCN B 201

Chain	Residue
B	LYS2
B	TYR5
B	ASN35
B	PHE38
B	GLU39
B	TYR114
B	ARG117
B	MET0
B	ARG1

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ALA102-VAL108

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

Chain	Residue	Details
A	ARG60-GLY82

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198

Chain	Residue	Details
C	SER5
C	SER7
D	SER5
D	SER7

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site_id	SWS_FT_FI2
Number of Residues	2
Details	MOD_RES: N6-succinyllysine => ECO:0000269|PubMed:22389435

Chain	Residue	Details
A	LYS11
B	LYS11

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site_id	SWS_FT_FI3
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:10642555, ECO:0000269|PubMed:12535538, ECO:0000269|PubMed:12535539, ECO:0000269|PubMed:14660635, ECO:0000269|PubMed:15280549, ECO:0000269|PubMed:16432255

Chain	Residue	Details
B	LYS88
A	LYS88

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