1WES

Solution structure of PHD domain in inhibitor of growth family, member 1-like

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 201

Chain	Residue
A	CYS19
A	CYS21
A	HIS43
A	CYS46

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site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 401

Chain	Residue
A	CYS32
A	CYS37
A	CYS59
A	CYS62

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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	CYS19-CYS62

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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	PRO16-ASP65

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

Chain	Residue	Details
A	CYS19
A	CYS21
A	CYS32
A	CYS37
A	HIS43
A	CYS46
A	CYS59
A	CYS62

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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	TYR18
A	MET29
A	ASP33
A	TRP41

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