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3LQJ

Crystal structure of MLL1 PHD3-Bromo complexed with H3(1-9)K4me3 peptide

Functional Information from GO Data
ChainGOidnamespacecontents
A0042800molecular_functionhistone methyltransferase activity (H3-K4 specific)
A0071339cellular_componentMLL1 complex
B0042800molecular_functionhistone methyltransferase activity (H3-K4 specific)
B0071339cellular_componentMLL1 complex
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 3
ChainResidue
ACYS1569
ACYS1572
AHIS1596
ACYS1599

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 4
ChainResidue
ACYS1588
ACYS1591
ACYS1621
ACYS1624

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1
ChainResidue
BCYS1572
BHIS1596
BCYS1599
BCYS1569

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 2
ChainResidue
BCYS1588
BCYS1591
BCYS1621
BCYS1624

Functional Information from PROSITE/UniProt
site_idPS01359
Number of Residues56
DetailsZF_PHD_1 Zinc finger PHD-type signature. CplCdkcyddddyeskm................................MqCgk..Cdrw.VHskCenlsdemyeilsnlpesva..........................YtCvnC
ChainResidueDetails
ACYS1569-CYS1624

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues122
DetailsZinc finger: {"description":"PHD-type 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00146","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues32
DetailsRegion: {"description":"Interaction with histone H3K4me3","evidences":[{"source":"PubMed","id":"20677832","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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