1WEU

Solution structure of PHD domain in ING1-like protein BAC25009

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	0016573	biological_process	histone acetylation
A	0070776	cellular_component	MOZ/MORF histone acetyltransferase complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 201

Chain	Residue
A	CYS39
A	CYS41
A	HIS63
A	CYS66

---

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

Chain	Residue
A	CYS52
A	CYS57
A	CYS79
A	CYS82

---

Functional Information from PROSITE/UniProt

site_id	PS01359
Number of Residues	44
Details	ZF_PHD_1 Zinc finger PHD-type signature. Cl.Chqvsygem.....................................IgCdnpdCsiewFHfaCvglttkprgk...................................WfCprC

Chain	Residue	Details
A	CYS39-CYS82

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	49
Details	Zinc finger: {"description":"PHD-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00146","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9UK53","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Site: {"description":"Histone H3K4me3 binding","evidences":[{"source":"UniProtKB","id":"Q9UK53","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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