3KQI

crystal structure of PHF2 PHD domain complexed with H3K4Me3 peptide

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0048188	cellular_component	Set1C/COMPASS complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 71

Chain	Residue
A	CYS23
A	CYS26
A	CYS50
A	CYS53

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site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 72

Chain	Residue
A	CYS8
A	CYS10
A	HIS31
A	CYS34

---

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 968

Chain	Residue
A	THR56
A	HIS57
A	HIS57
A	HOH83
A	HOH154
A	HOH154
A	CYS53

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site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL A 73

Chain	Residue
A	LYS64
A	HOH158
A	HOH167

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site_id	AC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE MG A 74

Chain	Residue
A	THR67

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site_id	AC6
Number of Residues	1
Details	BINDING SITE FOR RESIDUE MG A 75

Chain	Residue
A	SER33

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Functional Information from PROSITE/UniProt

site_id	PS01186
Number of Residues	16
Details	EGF_2 EGF-like domain signature 2. CvCrlPYdvtrfmieC

Chain	Residue	Details
A	CYS8-CYS23

---

site_id	PS01359
Number of Residues	46
Details	ZF_PHD_1 Zinc finger PHD-type signature. Cv.Crlpydvtrfm...................................IeCda..Ckdw.FHgsCvgveeeeapdidi................................YhCpnC

Chain	Residue	Details
A	CYS8-CYS53

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	51
Details	Zinc finger: {"description":"PHD-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00146","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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