5YC3

Crystal structure of AL3 PHD finger bound to H3K4me2

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0006355	biological_process	regulation of DNA-templated transcription
A	0042393	molecular_function	histone binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue ZN A 101

Chain	Residue
A	CYS7
A	CYS10
A	HIS31
A	CYS34

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site_id	AC2
Number of Residues	4
Details	binding site for residue ZN A 102

Chain	Residue
A	CYS23
A	CYS26
A	CYS50
A	CYS53

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site_id	AC3
Number of Residues	12
Details	binding site for Ligand residues MLY P 4 through GLN P 5 bound to THR P 3

Chain	Residue
A	ASP17
A	GLU18
A	PHE19
A	TRP20
A	TRP29
P	ALA1
P	ARG2
P	THR3
P	THR3
P	THR6
P	HOH101
A	ASP14

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Functional Information from PROSITE/UniProt

site_id	PS01359
Number of Residues	47
Details	ZF_PHD_1 Zinc finger PHD-type signature. CgaCgdsdgadefw...................................IcCdl..Cekw.FHgkCvkitparaehikq................................YkCpsC

Chain	Residue	Details
A	CYS7-CYS53

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	MOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:12581305, ECO:0000269|PubMed:14712277, ECO:0000269|PubMed:15598823, ECO:0000269|PubMed:16258034

Chain	Residue	Details
P	MLY4
A	ASP24
A	TRP29

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site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:12456661, ECO:0000269|PubMed:12581305, ECO:0000269|PubMed:14712277, ECO:0000269|PubMed:15014946, ECO:0000269|PubMed:15598823

Chain	Residue	Details
P	LYS9

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