5YC4

Crystal structure of AL3 PHD finger bound to H3K4me3

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

---

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

---

site_id	AC3
Number of Residues	11
Details	binding site for Ligand residues M3L P 4 through GLN P 5 bound to THR P 3

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

---

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

---

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	M3L4
A	ASP24
A	TRP29

---

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

---