2FUU

NMR solution structure of the PHD domain from the human BPTF in complex with H3(1-15)K4me3 peptide

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0006357	biological_process	regulation of transcription by RNA polymerase II
A	0016589	cellular_component	NURF complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ZN A 201

Chain	Residue
A	CYS26
A	ASP27
A	ARG28
A	CYS29
A	VAL52
A	CYS53
A	CYS56

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site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 202

Chain	Residue
A	HIS34
A	CYS37
A	CYS11
A	CYS13

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	CYS11-CYS26

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site_id	PS01359
Number of Residues	46
Details	ZF_PHD_1 Zinc finger PHD-type signature. Ci.Cktpydeskfy...................................IgCdr..Cqnw.YHgrCvgilqseaelide................................YvCpqC

Chain	Residue	Details
A	CYS11-CYS56

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	51
Details	ZN_FING: PHD-type 2 => ECO:0000255|PROSITE-ProRule:PRU00146

Chain	Residue	Details
A	LYS8-THR59
B	SER10

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site_id	SWS_FT_FI2
Number of Residues	4
Details	SITE: Histone H3K4me3 binding

Chain	Residue	Details
A	TYR10
A	TYR17
A	TYR23
A	TRP32

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: N6-acetyllysine; alternate => ECO:0000250

Chain	Residue	Details
B	ALA15

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