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6PWW

Cryo-EM structure of MLL1 in complex with RbBP5 and WDR5 bound to the nucleosome

Functional Information from GO Data
ChainGOidnamespacecontents
A0000976molecular_functiontranscription cis-regulatory region binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005730cellular_componentnucleolus
A0006325biological_processchromatin organization
A0006974biological_processDNA damage response
A0035097cellular_componenthistone methyltransferase complex
A0042393molecular_functionhistone binding
A0043627biological_processresponse to estrogen
A0044665cellular_componentMLL1/2 complex
A0044666cellular_componentMLL3/4 complex
A0045815biological_processtranscription initiation-coupled chromatin remodeling
A0048188cellular_componentSet1C/COMPASS complex
A0071339cellular_componentMLL1 complex
B0000122biological_processnegative regulation of transcription by RNA polymerase II
B0000123cellular_componenthistone acetyltransferase complex
B0001501biological_processskeletal system development
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0006094biological_processgluconeogenesis
B0006325biological_processchromatin organization
B0006355biological_processregulation of DNA-templated transcription
B0006357biological_processregulation of transcription by RNA polymerase II
B0035097cellular_componenthistone methyltransferase complex
B0042393molecular_functionhistone binding
B0042800molecular_functionhistone H3K4 methyltransferase activity
B0044545cellular_componentNSL complex
B0044665cellular_componentMLL1/2 complex
B0044666cellular_componentMLL3/4 complex
B0045722biological_processpositive regulation of gluconeogenesis
B0045815biological_processtranscription initiation-coupled chromatin remodeling
B0045893biological_processpositive regulation of DNA-templated transcription
B0045995biological_processregulation of embryonic development
B0048188cellular_componentSet1C/COMPASS complex
B0051302biological_processregulation of cell division
B0051726biological_processregulation of cell cycle
B0071339cellular_componentMLL1 complex
B0072686cellular_componentmitotic spindle
B0140004molecular_functionhistone H3Q5ser reader activity
B0140109molecular_functionhistone H3K4me1 reader activity
B0140672cellular_componentATAC complex
G0000786cellular_componentnucleosome
G0003677molecular_functionDNA binding
G0005515molecular_functionprotein binding
G0005634cellular_componentnucleus
G0005654cellular_componentnucleoplasm
G0005694cellular_componentchromosome
G0030527molecular_functionstructural constituent of chromatin
G0046982molecular_functionprotein heterodimerization activity
H0000786cellular_componentnucleosome
H0003677molecular_functionDNA binding
H0005515molecular_functionprotein binding
H0005634cellular_componentnucleus
H0005694cellular_componentchromosome
H0006334biological_processnucleosome assembly
H0030527molecular_functionstructural constituent of chromatin
H0046982molecular_functionprotein heterodimerization activity
I0000786cellular_componentnucleosome
I0003677molecular_functionDNA binding
I0005634cellular_componentnucleus
I0005694cellular_componentchromosome
I0030527molecular_functionstructural constituent of chromatin
I0031507biological_processheterochromatin formation
I0046982molecular_functionprotein heterodimerization activity
J0000786cellular_componentnucleosome
J0003677molecular_functionDNA binding
J0005515molecular_functionprotein binding
J0005634cellular_componentnucleus
J0005694cellular_componentchromosome
J0030527molecular_functionstructural constituent of chromatin
J0046982molecular_functionprotein heterodimerization activity
K0000786cellular_componentnucleosome
K0003677molecular_functionDNA binding
K0005515molecular_functionprotein binding
K0005634cellular_componentnucleus
K0005654cellular_componentnucleoplasm
K0005694cellular_componentchromosome
K0030527molecular_functionstructural constituent of chromatin
K0046982molecular_functionprotein heterodimerization activity
L0000786cellular_componentnucleosome
L0003677molecular_functionDNA binding
L0005515molecular_functionprotein binding
L0005634cellular_componentnucleus
L0005694cellular_componentchromosome
L0006334biological_processnucleosome assembly
L0030527molecular_functionstructural constituent of chromatin
L0046982molecular_functionprotein heterodimerization activity
M0000786cellular_componentnucleosome
M0003677molecular_functionDNA binding
M0005634cellular_componentnucleus
M0005694cellular_componentchromosome
M0030527molecular_functionstructural constituent of chromatin
M0031507biological_processheterochromatin formation
M0046982molecular_functionprotein heterodimerization activity
N0000786cellular_componentnucleosome
N0003677molecular_functionDNA binding
N0005515molecular_functionprotein binding
N0005634cellular_componentnucleus
N0005694cellular_componentchromosome
N0030527molecular_functionstructural constituent of chromatin
N0046982molecular_functionprotein heterodimerization activity
Functional Information from PDB Data
site_idAC1
Number of Residues16
Detailsbinding site for residue SAH C 4001
ChainResidue
CILE3838
CHIS3907
CTYR3944
CLEU3955
CPRO3956
CCYS3957
CASN3958
CLEU3968
CHIS3839
CGLY3840
CARG3841
CTYR3883
CARG3903
CPHE3904
CILE3905
CASN3906

site_idAC2
Number of Residues5
Detailsbinding site for residue ZN C 4002
ChainResidue
CSER3908
CCYS3909
CCYS3957
CCYS3959
CCYS3964

Functional Information from PROSITE/UniProt
site_idPS00046
Number of Residues7
DetailsHISTONE_H2A Histone H2A signature. AGLqFPV
ChainResidueDetails
IALA21-VAL27

site_idPS00047
Number of Residues5
DetailsHISTONE_H4 Histone H4 signature. GAKRH
ChainResidueDetails
HGLY14-HIS18

site_idPS00322
Number of Residues7
DetailsHISTONE_H3_1 Histone H3 signature 1. KAPRKQL
ChainResidueDetails
GLYS14-LEU20

site_idPS00357
Number of Residues23
DetailsHISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG
ChainResidueDetails
JARG89-GLY111

site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. LVSAsdDkTLKIWDV
ChainResidueDetails
BLEU102-VAL116
BILE144-VAL158
BILE186-THR200
BILE274-LEU288

site_idPS00959
Number of Residues9
DetailsHISTONE_H3_2 Histone H3 signature 2. PFqRLVREI
ChainResidueDetails
GPRO66-ILE74

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues80
DetailsRepeat: {"description":"WD 1"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues80
DetailsRepeat: {"description":"WD 2"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues80
DetailsRepeat: {"description":"WD 3"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues78
DetailsRepeat: {"description":"WD 4"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues83
DetailsRepeat: {"description":"WD 5"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues78
DetailsRepeat: {"description":"WD 6"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by CDK1","evidences":[{"source":"PubMed","id":"7558034","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17081983","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues34
DetailsRepeat: {"description":"WD 7"}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues4
DetailsSite: {"description":"Important for interaction with histone H3"}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues116
DetailsDomain: {"description":"SET","evidences":[{"source":"PROSITE-ProRule","id":"PRU00190","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00190","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19187761","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26886794","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2W5Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5F5E","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5F6L","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00190","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19187761","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26886794","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2W5Z","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5F5E","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19187761","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26886794","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2W5Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5F5E","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5F6L","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16990798","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19187761","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2W5Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2W5Z","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5F5E","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5F6L","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16990798","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19187761","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2W5Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2W5Z","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5F6L","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI19
Number of Residues1
DetailsModified residue: {"description":"S-methylcysteine; by autocatalysis","evidences":[{"source":"PubMed","id":"24235145","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI20
Number of Residues2
DetailsModified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P68431","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI21
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI22
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P84228","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI23
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI24
Number of Residues2
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI25
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI26
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P84243","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI27
Number of Residues2
DetailsModified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI28
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI29
Number of Residues2
DetailsLipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI30
Number of Residues2
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI31
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI32
Number of Residues4
DetailsModified residue: {"description":"N6-propionyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI33
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by PAK2","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI34
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI35
Number of Residues2
DetailsModified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI36
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI37
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI38
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI39
Number of Residues2
DetailsModified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine; alternate","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI40
Number of Residues4
DetailsModified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI41
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI42
Number of Residues2
DetailsModified residue: {"description":"N5-methylglutamine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI43
Number of Residues2
DetailsModified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI44
Number of Residues6
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI45
Number of Residues2
DetailsGlycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"source":"UniProtKB","id":"P62807","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI46
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P0C1H4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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