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6R25

Structure of LSD2/NPAC-linker/nucleosome core particle complex: Class 3

Functional Information from GO Data
ChainGOidnamespacecontents
A0000786cellular_componentnucleosome
A0003677molecular_functionDNA binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005694cellular_componentchromosome
A0030527molecular_functionstructural constituent of chromatin
A0046982molecular_functionprotein heterodimerization activity
B0000786cellular_componentnucleosome
B0003677molecular_functionDNA binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005694cellular_componentchromosome
B0006334biological_processnucleosome assembly
B0030527molecular_functionstructural constituent of chromatin
B0046982molecular_functionprotein heterodimerization activity
C0000786cellular_componentnucleosome
C0003677molecular_functionDNA binding
C0005634cellular_componentnucleus
C0005694cellular_componentchromosome
C0030527molecular_functionstructural constituent of chromatin
C0046982molecular_functionprotein heterodimerization activity
D0000786cellular_componentnucleosome
D0003677molecular_functionDNA binding
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005694cellular_componentchromosome
D0030527molecular_functionstructural constituent of chromatin
D0046982molecular_functionprotein heterodimerization activity
E0000786cellular_componentnucleosome
E0003677molecular_functionDNA binding
E0005515molecular_functionprotein binding
E0005634cellular_componentnucleus
E0005654cellular_componentnucleoplasm
E0005694cellular_componentchromosome
E0030527molecular_functionstructural constituent of chromatin
E0046982molecular_functionprotein heterodimerization activity
F0000786cellular_componentnucleosome
F0003677molecular_functionDNA binding
F0005515molecular_functionprotein binding
F0005634cellular_componentnucleus
F0005694cellular_componentchromosome
F0006334biological_processnucleosome assembly
F0030527molecular_functionstructural constituent of chromatin
F0046982molecular_functionprotein heterodimerization activity
G0000786cellular_componentnucleosome
G0003677molecular_functionDNA binding
G0005634cellular_componentnucleus
G0005694cellular_componentchromosome
G0030527molecular_functionstructural constituent of chromatin
G0046982molecular_functionprotein heterodimerization activity
H0000786cellular_componentnucleosome
H0003677molecular_functionDNA binding
H0005515molecular_functionprotein binding
H0005634cellular_componentnucleus
H0005694cellular_componentchromosome
H0030527molecular_functionstructural constituent of chromatin
H0046982molecular_functionprotein heterodimerization activity
K0000786cellular_componentnucleosome
K0003682molecular_functionchromatin binding
K0005515molecular_functionprotein binding
K0005634cellular_componentnucleus
K0005654cellular_componentnucleoplasm
K0005694cellular_componentchromosome
K0006325biological_processchromatin organization
K0006338biological_processchromatin remodeling
K0008270molecular_functionzinc ion binding
K0016491molecular_functionoxidoreductase activity
K0032452molecular_functionhistone demethylase activity
K0032453molecular_functionhistone H3K4 demethylase activity
K0042393molecular_functionhistone binding
K0044726biological_processepigenetic programing of female pronucleus
K0046872molecular_functionmetal ion binding
K0050660molecular_functionflavin adenine dinucleotide binding
K0071514biological_processgenomic imprinting
K0071949molecular_functionFAD binding
K0140682molecular_functionFAD-dependent H3K4me/H3K4me3 demethylase activity
M0000786cellular_componentnucleosome
M0003677molecular_functionDNA binding
M0005515molecular_functionprotein binding
M0005634cellular_componentnucleus
M0005654cellular_componentnucleoplasm
M0005694cellular_componentchromosome
M0030527molecular_functionstructural constituent of chromatin
M0046982molecular_functionprotein heterodimerization activity
Functional Information from PDB Data
site_idAC1
Number of Residues32
Detailsbinding site for residue FAD K 901
ChainResidue
KILE388
KGLY419
KARG420
KARG434
KGLY435
KALA436
KILE438
KVAL598
KVAL627
KPRO628
KTRP757
KGLY389
KTRP762
KALA766
KGLY794
KGLU795
KGLN803
KTHR804
KVAL805
KALA808
KHOH1058
KHOH1062
KGLY391
KHOH1119
KHOH1125
KHOH1128
KPRO392
KALA393
KLEU411
KGLU412
KALA413
KLYS414

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN K 902
ChainResidue
KCYS53
KCYS58
KHIS84
KHIS90

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN K 903
ChainResidue
KCYS65
KCYS73
KCYS92
KCYS95

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN K 904
ChainResidue
KCYS142
KCYS147
KCYS169
KCYS185

Functional Information from PROSITE/UniProt
site_idPS00046
Number of Residues7
DetailsHISTONE_H2A Histone H2A signature. AGLqFPV
ChainResidueDetails
CALA21-VAL27

site_idPS00047
Number of Residues5
DetailsHISTONE_H4 Histone H4 signature. GAKRH
ChainResidueDetails
BGLY14-HIS18

site_idPS00322
Number of Residues7
DetailsHISTONE_H3_1 Histone H3 signature 1. KAPRKQL
ChainResidueDetails
MLYS14-LEU20
ALYS14-LEU20

site_idPS00959
Number of Residues9
DetailsHISTONE_H3_2 Histone H3 signature 2. PFqRLVREI
ChainResidueDetails
MPRO66-ILE74
APRO66-ILE74

site_idPS00357
Number of Residues23
DetailsHISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG
ChainResidueDetails
DARG89-GLY111

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: Citrulline; alternate => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
MARG2
MARG17
DLYS12
DLYS17
HLYS2
HLYS9
HLYS12
HLYS17

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by HASPIN => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
KCYS65
KCYS73
KHIS84
KHIS90
KCYS92
KCYS95
KVAL598
KGLN803
MTHR3
HSER11

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:12138181
ChainResidueDetails
HSER109
GLYS9
GLYS95
MMET4

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: 5-glutamyl serotonin; alternate => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
GLYS36
HLYS117
MGLN5

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by PKC => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
MTHR6
MTHR11
GLYS74
GLYS75
FLYS8
FLYS16
FLYS44
FLYS79

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000250
ChainResidueDetails
MARG8
GGLN104
FLYS12
FLYS20

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000305|PubMed:12138181
ChainResidueDetails
MLYS9
GLYS118
FLYS31
FLYS91

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
GLYS15
GLYS119
MSER10
FSER47
CLYS15
CLYS119
GLYS13

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: N6-lactoyllysine; alternate => ECO:0000250|UniProtKB:P84228
ChainResidueDetails
MLYS14
BTYR88
FTYR51
FTYR88

site_idSWS_FT_FI10
Number of Residues5
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
MLYS27
MLYS36
MLYS64
ELYS18
ELYS23
ELYS27
ELYS36
ELYS64
MLYS18
MLYS23

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Citrulline => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
MARG26
FLYS77

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphoserine; alternate; by AURKB, AURKC and RPS6KA5 => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
MSER28
FLYS31

site_idSWS_FT_FI13
Number of Residues1
DetailsMOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68431
ChainResidueDetails
MLYS37
BLYS91
FLYS91

site_idSWS_FT_FI14
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
MTYR41
ETYR41

site_idSWS_FT_FI15
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228
ChainResidueDetails
MLYS56
MLYS79
ELYS56
ELYS79

site_idSWS_FT_FI16
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
MSER57
ESER57

site_idSWS_FT_FI17
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ETHR80
ETHR107
MTHR80
MTHR107

site_idSWS_FT_FI18
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P84243
ChainResidueDetails
MSER86
ESER86

site_idSWS_FT_FI19
Number of Residues1
DetailsMOD_RES: N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
MLYS115
ELYS115

site_idSWS_FT_FI20
Number of Residues1
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
MLYS122
ELYS122

site_idSWS_FT_FI21
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
MCYS110
ECYS110

219869

PDB entries from 2024-05-15

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