2G6Q

Crystal structure of ING2 PHD finger in complex with H3K4Me3 peptide

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003682	molecular_function	chromatin binding
A	0005634	cellular_component	nucleus
A	0006325	biological_process	chromatin organization
A	0008285	biological_process	negative regulation of cell population proliferation
A	0042981	biological_process	regulation of apoptotic process
A	2000772	biological_process	regulation of cellular senescence

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 300

Chain	Residue
A	CYS216
A	CYS218
A	HIS240
A	CYS243

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site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 400

Chain	Residue
A	CYS229
A	CYS234
A	CYS256
A	CYS259

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Functional Information from PROSITE/UniProt

site_id	PS01359
Number of Residues	44
Details	ZF_PHD_1 Zinc finger PHD-type signature. Cl.Cnqvsygem.....................................IgCdneqCpiewFHfsCvsltykpkgk...................................WyCpkC

Chain	Residue	Details
A	CYS216-CYS259

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	49
Details	ZN_FING: PHD-type => ECO:0000255|PROSITE-ProRule:PRU00146

Chain	Residue	Details
A	PRO213-ASP262

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site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000250|UniProtKB:Q9UK53

Chain	Residue	Details
A	CYS216
A	CYS218
A	CYS229
A	CYS234
A	HIS240
A	CYS243
A	CYS256
A	CYS259

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site_id	SWS_FT_FI3
Number of Residues	4
Details	SITE: Histone H3K4me3 binding => ECO:0000250|UniProtKB:Q9UK53

Chain	Residue	Details
A	TYR215
A	MET226
A	ASP230
A	TRP238

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