Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6W5I

Cryo-EM structure of MLL1 in complex with RbBP5, WDR5, SET1, and ASH2L bound to the nucleosome (Class01)

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
B0035064molecular_functionmethylated histone binding
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
B0090043biological_processregulation of tubulin deacetylation
B0140672cellular_componentATAC complex
D0048188cellular_componentSet1C/COMPASS 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
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
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 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 Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250
ChainResidueDetails
ISER1
MSER1
JLYS12
JLYS17
NLYS2
NLYS9
NLYS12
NLYS17

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250
ChainResidueDetails
ILYS5
MLYS5

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P0C0S8
ChainResidueDetails
ILYS9
ILYS95
MLYS9
MLYS95

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-(2-hydroxyisobutyryl)lysine; alternate => ECO:0000250|UniProtKB:P0C0S8
ChainResidueDetails
ILYS36
MLYS36
NLYS117

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8
ChainResidueDetails
ILYS74
ILYS75
MLYS74
MLYS75
LLYS8
LLYS16
LLYS44
LLYS79

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N5-methylglutamine => ECO:0000250
ChainResidueDetails
IGLN104
MGLN104
LLYS12
LLYS20

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8
ChainResidueDetails
ILYS118
MLYS118
LLYS31
LLYS91

site_idSWS_FT_FI8
Number of Residues8
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250
ChainResidueDetails
ILYS13
LSER47
ILYS15
ILYS119
MLYS13
MLYS15
MLYS119

site_idSWS_FT_FI9
Number of Residues4
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P62805
ChainResidueDetails
HTYR51
HTYR88
LTYR51
LTYR88

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805
ChainResidueDetails
HLYS59
KLYS64
LLYS59
GLYS27
GLYS36
GLYS64
KLYS18
KLYS23
KLYS27
KLYS36

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P62805
ChainResidueDetails
HLYS77
LLYS77

site_idSWS_FT_FI12
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate => ECO:0000250|UniProtKB:P62805
ChainResidueDetails
HLYS31
LLYS31

site_idSWS_FT_FI13
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62805
ChainResidueDetails
GLYS37
HLYS91
LLYS91

site_idSWS_FT_FI14
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
GTYR41
KTYR41

site_idSWS_FT_FI15
Number of Residues4
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228
ChainResidueDetails
GLYS56
GLYS79
KLYS56
KLYS79

site_idSWS_FT_FI16
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
GSER57
KSER57

site_idSWS_FT_FI17
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
GTHR80
GTHR107
KTHR80
KTHR107

site_idSWS_FT_FI18
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P84243
ChainResidueDetails
GSER86
KSER86

site_idSWS_FT_FI19
Number of Residues2
DetailsMOD_RES: N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
GLYS115
KLYS115

site_idSWS_FT_FI20
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
GLYS122
KLYS122

site_idSWS_FT_FI21
Number of Residues2
DetailsLIPID: S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
GCYS110
KCYS110

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon