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3LEL

Structural Insight into the Sequence-Dependence of Nucleosome Positioning

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
A0031492molecular_functionnucleosomal DNA binding
A0031507biological_processheterochromatin formation
A0046982molecular_functionprotein heterodimerization activity
B0000786cellular_componentnucleosome
B0003677molecular_functionDNA binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005694cellular_componentchromosome
B0006334biological_processnucleosome assembly
B0030527molecular_functionstructural constituent of chromatin
B0031507biological_processheterochromatin formation
B0046982molecular_functionprotein heterodimerization activity
C0000786cellular_componentnucleosome
C0003677molecular_functionDNA binding
C0005634cellular_componentnucleus
C0005694cellular_componentchromosome
C0030527molecular_functionstructural constituent of chromatin
C0031507biological_processheterochromatin formation
C0046982molecular_functionprotein heterodimerization activity
D0000786cellular_componentnucleosome
D0002227biological_processinnate immune response in mucosa
D0003677molecular_functionDNA binding
D0005515molecular_functionprotein binding
D0005615cellular_componentextracellular space
D0005634cellular_componentnucleus
D0005694cellular_componentchromosome
D0006325biological_processchromatin organization
D0019731biological_processantibacterial humoral response
D0030527molecular_functionstructural constituent of chromatin
D0031507biological_processheterochromatin formation
D0046982molecular_functionprotein heterodimerization activity
D0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
E0000786cellular_componentnucleosome
E0003677molecular_functionDNA binding
E0005515molecular_functionprotein binding
E0005634cellular_componentnucleus
E0005654cellular_componentnucleoplasm
E0005694cellular_componentchromosome
E0030527molecular_functionstructural constituent of chromatin
E0031492molecular_functionnucleosomal DNA binding
E0031507biological_processheterochromatin formation
E0046982molecular_functionprotein heterodimerization activity
F0000786cellular_componentnucleosome
F0003677molecular_functionDNA binding
F0005515molecular_functionprotein binding
F0005634cellular_componentnucleus
F0005694cellular_componentchromosome
F0006334biological_processnucleosome assembly
F0030527molecular_functionstructural constituent of chromatin
F0031507biological_processheterochromatin formation
F0046982molecular_functionprotein heterodimerization activity
G0000786cellular_componentnucleosome
G0003677molecular_functionDNA binding
G0005634cellular_componentnucleus
G0005694cellular_componentchromosome
G0030527molecular_functionstructural constituent of chromatin
G0031507biological_processheterochromatin formation
G0046982molecular_functionprotein heterodimerization activity
H0000786cellular_componentnucleosome
H0002227biological_processinnate immune response in mucosa
H0003677molecular_functionDNA binding
H0005515molecular_functionprotein binding
H0005615cellular_componentextracellular space
H0005634cellular_componentnucleus
H0005694cellular_componentchromosome
H0006325biological_processchromatin organization
H0019731biological_processantibacterial humoral response
H0030527molecular_functionstructural constituent of chromatin
H0031507biological_processheterochromatin formation
H0046982molecular_functionprotein heterodimerization activity
H0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
K0000786cellular_componentnucleosome
K0003677molecular_functionDNA binding
K0005515molecular_functionprotein binding
K0005634cellular_componentnucleus
K0005654cellular_componentnucleoplasm
K0005694cellular_componentchromosome
K0030527molecular_functionstructural constituent of chromatin
K0031492molecular_functionnucleosomal DNA binding
K0031507biological_processheterochromatin formation
K0046982molecular_functionprotein heterodimerization activity
L0000786cellular_componentnucleosome
L0003677molecular_functionDNA binding
L0005515molecular_functionprotein binding
L0005634cellular_componentnucleus
L0005694cellular_componentchromosome
L0006334biological_processnucleosome assembly
L0030527molecular_functionstructural constituent of chromatin
L0031507biological_processheterochromatin formation
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
N0002227biological_processinnate immune response in mucosa
N0003677molecular_functionDNA binding
N0005515molecular_functionprotein binding
N0005615cellular_componentextracellular space
N0005634cellular_componentnucleus
N0005694cellular_componentchromosome
N0006325biological_processchromatin organization
N0019731biological_processantibacterial humoral response
N0030527molecular_functionstructural constituent of chromatin
N0031507biological_processheterochromatin formation
N0046982molecular_functionprotein heterodimerization activity
N0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
O0000786cellular_componentnucleosome
O0003677molecular_functionDNA binding
O0005515molecular_functionprotein binding
O0005634cellular_componentnucleus
O0005654cellular_componentnucleoplasm
O0005694cellular_componentchromosome
O0030527molecular_functionstructural constituent of chromatin
O0031492molecular_functionnucleosomal DNA binding
O0031507biological_processheterochromatin formation
O0046982molecular_functionprotein heterodimerization activity
P0000786cellular_componentnucleosome
P0003677molecular_functionDNA binding
P0005515molecular_functionprotein binding
P0005634cellular_componentnucleus
P0005694cellular_componentchromosome
P0006334biological_processnucleosome assembly
P0030527molecular_functionstructural constituent of chromatin
P0031507biological_processheterochromatin formation
P0046982molecular_functionprotein heterodimerization activity
Q0000786cellular_componentnucleosome
Q0003677molecular_functionDNA binding
Q0005634cellular_componentnucleus
Q0005694cellular_componentchromosome
Q0030527molecular_functionstructural constituent of chromatin
Q0031507biological_processheterochromatin formation
Q0046982molecular_functionprotein heterodimerization activity
R0000786cellular_componentnucleosome
R0002227biological_processinnate immune response in mucosa
R0003677molecular_functionDNA binding
R0005515molecular_functionprotein binding
R0005615cellular_componentextracellular space
R0005634cellular_componentnucleus
R0005694cellular_componentchromosome
R0006325biological_processchromatin organization
R0019731biological_processantibacterial humoral response
R0030527molecular_functionstructural constituent of chromatin
R0031507biological_processheterochromatin formation
R0046982molecular_functionprotein heterodimerization activity
R0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MN N 3132
ChainResidue
NGLU102

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MN O 3152
ChainResidue
DVAL45
OASP77

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MN T 3134
ChainResidue
TDG61

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MN J 3135
ChainResidue
JDG27
SDT67

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MN I 3136
ChainResidue
IDG27

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MN J 3137
ChainResidue
JDG61

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MN J 3138
ChainResidue
JDG48

site_idAC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MN T 3139
ChainResidue
TDG64

site_idAC9
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MN G 3140
ChainResidue
GGLU91

site_idBC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MN I 3142
ChainResidue
IDG61

site_idBC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MN T 3143
ChainResidue
TDG27

site_idBC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MN I 3144
ChainResidue
IDG-2

site_idBC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MN T 3145
ChainResidue
TDT67
TDA68

site_idBC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MN S 3146
ChainResidue
SDG64
SDG65

site_idBC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MN T 3147
ChainResidue
TDA-3
TDG-2

site_idBC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MN J 3148
ChainResidue
JDG64

site_idBC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MN J 3149
ChainResidue
JDG-2

site_idBC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MN I 3150
ChainResidue
IDG-35
IDG-34

site_idCC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MN S 3151
ChainResidue
SDG-2

site_idCC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MN S 3153
ChainResidue
SDG61

site_idCC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MN T 3154
ChainResidue
TDG-56
TDA-57

site_idCC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MN S 3155
ChainResidue
SDT47
SDG48

site_idCC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MN T 3156
ChainResidue
TDG-34
TDG-35

site_idCC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MN S 3157
ChainResidue
SDA26
SDG27

site_idCC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MN S 3158
ChainResidue
SDG-35
SDG-34

site_idCC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MN T 3159
ChainResidue
TDG48
TDG49

site_idCC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MN I 3160
ChainResidue
IDT63
IDG64
IDG65

site_idDC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MN I 3161
ChainResidue
IDG48

site_idDC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MN T 3162
ChainResidue
TDT5

site_idDC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MN J 3164
ChainResidue
JDG64
JDG65
JDA66

site_idDC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MN J 3165
ChainResidue
JDT5

site_idDC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MN J 3166
ChainResidue
IDT4
JDA-3

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
ALYS14-LEU20

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

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P84228","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues8
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P84243","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsModified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues4
DetailsLipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P68431","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues8
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues9
DetailsModified residue: {"description":"N6-propionyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine; by PAK2","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues8
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues4
DetailsModified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues4
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_FI18
Number of Residues8
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_FI19
Number of Residues2
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI20
Number of Residues4
DetailsDNA binding: {}
ChainResidueDetails

site_idSWS_FT_FI21
Number of Residues4
DetailsGlycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"source":"UniProtKB","id":"P62807","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI22
Number of Residues8
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P0C1H4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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