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6O7G

Solution structure of MLL4 PHD6 domain in complex with histone H4K16ac peptide

Functional Information from GO Data
ChainGOidnamespacecontents
B0035097cellular_componenthistone methyltransferase complex
B0042800molecular_functionhistone methyltransferase activity (H3-K4 specific)
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN B 1601
ChainResidue
BCYS1507
BCYS1510
BHIS1531
BCYS1534

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN B 1602
ChainResidue
BCYS1523
BCYS1526
BCYS1553
BCYS1556

Functional Information from PROSITE/UniProt
site_idPS00047
Number of Residues5
DetailsHISTONE_H4 Histone H4 signature. GAKRH
ChainResidueDetails
AGLY14-HIS18

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues55
DetailsZinc finger: {"description":"PHD-type 6","evidences":[{"source":"PROSITE-ProRule","id":"PRU00146","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues50
DetailsZinc finger: {"description":"RING-type 3; atypical","evidences":[{"source":"PROSITE-ProRule","id":"PRU00175","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

262786

PDB entries from 2026-11-11

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