2YSM

Solution structure of the second and third PHD domain from Histone-lysine N-methyltransferase 2C (KMT2C/MLL3)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0042800	molecular_function	histone methyltransferase activity (H3-K4 specific)
A	0044666	cellular_component	MLL3/4 complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 301

Chain	Residue
A	CYS10
A	CYS13
A	HIS33
A	CYS36

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site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 501

Chain	Residue
A	CYS25
A	CYS28
A	CYS51
A	CYS54

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site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 701

Chain	Residue
A	CYS60
A	HIS80
A	CYS83
A	CYS57

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site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 901

Chain	Residue
A	CYS72
A	CYS75
A	CYS98
A	CYS101

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Functional Information from PROSITE/UniProt

site_id	PS01359
Number of Residues	66
Details	ZF_PHD_1 Zinc finger PHD-type signature. CavCdspgdlldq....................................FfCtt..Cgqh.YHgmCldiavtplkragwqcpeckvcqnckqsgedskm............LvCdtC

Chain	Residue	Details
A	CYS10-CYS75
A	CYS25-CYS101

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	45
Details	ZN_FING: RING-type => ECO:0000255|PROSITE-ProRule:PRU00175

Chain	Residue	Details
A	CYS10-LYS55

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site_id	SWS_FT_FI2
Number of Residues	50
Details	ZN_FING: PHD-type 3 => ECO:0000255|PROSITE-ProRule:PRU00146

Chain	Residue	Details
A	CYS54-CYS104

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