2QIC

Crystal Structure of the ING1 PHD Finger in complex with a Histone H3K4ME3 peptide

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005634	cellular_component	nucleus
A	0008285	biological_process	negative regulation of cell population proliferation
A	0010941	biological_process	regulation of cell death

Functional Information from PDB Data

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

Chain	Residue
A	CYS213
A	CYS215
A	HIS237
A	CYS240

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

Chain	Residue
A	CYS226
A	CYS231
A	CYS253
A	CYS256

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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.....................................IgCdndeCpiewFHfsCvglnhkpkgk...................................WyCpkC

Chain	Residue	Details
A	CYS213-CYS256

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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	PRO210-GLU259

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site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:18533182, ECO:0007744|PDB:2QIC

Chain	Residue	Details
A	CYS213
A	CYS215
A	CYS226
A	CYS231
A	HIS237
A	CYS240
A	CYS253
A	CYS256

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site_id	SWS_FT_FI3
Number of Residues	4
Details	SITE: Histone H3K4me3 binding => ECO:0000269|PubMed:18533182, ECO:0007744|PDB:2QIC

Chain	Residue	Details
A	TYR212
A	MET223
A	ASP227
A	TRP235

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