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5B1L

The mouse nucleosome structure containing H3t

Functional Information from GO Data
ChainGOidnamespacecontents
A0000786cellular_componentnucleosome
A0003677molecular_functionDNA binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005694cellular_componentchromosome
A0006325biological_processchromatin organization
A0030527molecular_functionstructural constituent of chromatin
A0046982molecular_functionprotein heterodimerization activity
B0000786cellular_componentnucleosome
B0003677molecular_functionDNA binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005694cellular_componentchromosome
B0006325biological_processchromatin organization
B0006334biological_processnucleosome assembly
B0030527molecular_functionstructural constituent of chromatin
B0043505cellular_componentCENP-A containing nucleosome
B0046982molecular_functionprotein heterodimerization activity
B0061644biological_processprotein localization to CENP-A containing chromatin
C0000786cellular_componentnucleosome
C0003677molecular_functionDNA binding
C0005634cellular_componentnucleus
C0005694cellular_componentchromosome
C0006325biological_processchromatin organization
C0030527molecular_functionstructural constituent of chromatin
C0031492molecular_functionnucleosomal DNA binding
C0043505cellular_componentCENP-A containing nucleosome
C0046982molecular_functionprotein heterodimerization activity
C0061644biological_processprotein localization to CENP-A containing chromatin
C0070828biological_processheterochromatin organization
D0000786cellular_componentnucleosome
D0003677molecular_functionDNA binding
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
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
E0006325biological_processchromatin organization
E0030527molecular_functionstructural constituent of chromatin
E0046982molecular_functionprotein heterodimerization activity
F0000786cellular_componentnucleosome
F0003677molecular_functionDNA binding
F0005515molecular_functionprotein binding
F0005634cellular_componentnucleus
F0005654cellular_componentnucleoplasm
F0005694cellular_componentchromosome
F0006325biological_processchromatin organization
F0006334biological_processnucleosome assembly
F0030527molecular_functionstructural constituent of chromatin
F0043505cellular_componentCENP-A containing nucleosome
F0046982molecular_functionprotein heterodimerization activity
F0061644biological_processprotein localization to CENP-A containing chromatin
G0000786cellular_componentnucleosome
G0003677molecular_functionDNA binding
G0005634cellular_componentnucleus
G0005694cellular_componentchromosome
G0006325biological_processchromatin organization
G0030527molecular_functionstructural constituent of chromatin
G0031492molecular_functionnucleosomal DNA binding
G0043505cellular_componentCENP-A containing nucleosome
G0046982molecular_functionprotein heterodimerization activity
G0061644biological_processprotein localization to CENP-A containing chromatin
G0070828biological_processheterochromatin organization
H0000786cellular_componentnucleosome
H0003677molecular_functionDNA binding
H0005634cellular_componentnucleus
H0005654cellular_componentnucleoplasm
H0005694cellular_componentchromosome
H0030527molecular_functionstructural constituent of chromatin
H0046982molecular_functionprotein heterodimerization activity
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue CL A 301
ChainResidue
APRO121
ALYS122

site_idAC2
Number of Residues5
Detailsbinding site for residue CL C 301
ChainResidue
CGLY44
CGLY46
CALA47
DTHR90
DSER91

site_idAC3
Number of Residues6
Detailsbinding site for residue MN D 301
ChainResidue
DHOH402
DHOH409
EASP77
EHOH412
CHOH409
DVAL48

site_idAC4
Number of Residues2
Detailsbinding site for residue CL E 301
ChainResidue
EPRO121
ELYS122

site_idAC5
Number of Residues4
Detailsbinding site for residue CL G 301
ChainResidue
GGLY44
GGLY46
GALA47
HSER91

site_idAC6
Number of Residues3
Detailsbinding site for residue MN I 301
ChainResidue
IDG121
IHOH406
IHOH435

site_idAC7
Number of Residues4
Detailsbinding site for residue MN I 302
ChainResidue
IHOH414
IHOH441
JHOH511
JHOH538

site_idAC8
Number of Residues3
Detailsbinding site for residue MN I 303
ChainResidue
IDG134
IHOH432
IHOH437

site_idAC9
Number of Residues3
Detailsbinding site for residue MN I 304
ChainResidue
IDG68
IHOH409
JHOH517

site_idAD1
Number of Residues2
Detailsbinding site for residue MN I 305
ChainResidue
IHOH419
JHOH540

site_idAD2
Number of Residues1
Detailsbinding site for residue MN I 306
ChainResidue
IDA17

site_idAD3
Number of Residues5
Detailsbinding site for residue MN J 401
ChainResidue
JDG267
JHOH505
JHOH532
JHOH537
JHOH545

site_idAD4
Number of Residues5
Detailsbinding site for residue MN J 402
ChainResidue
JDG185
JDG186
JHOH522
JHOH530
JHOH531

site_idAD5
Number of Residues3
Detailsbinding site for residue MN J 403
ChainResidue
JDG280
JHOH519
JHOH544

site_idAD6
Number of Residues2
Detailsbinding site for residue MN J 404
ChainResidue
JDT183
JHOH541

site_idAD7
Number of Residues2
Detailsbinding site for residue MN J 405
ChainResidue
JDG217
JHOH502

site_idAD8
Number of Residues1
Detailsbinding site for residue MN J 406
ChainResidue
JHOH542

Functional Information from PROSITE/UniProt
site_idPS00322
Number of Residues7
DetailsHISTONE_H3_1 Histone H3 signature 1. KAPRKQL
ChainResidueDetails
ALYS14-LEU20

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

site_idPS00357
Number of Residues23
DetailsHISTONE_H2B Histone H2B signature. REVQTavRlLLpGELaKHAVSEG
ChainResidueDetails
DARG92-GLY114

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: Phosphoarginine; alternate => ECO:0000305
ChainResidueDetails
AARG2
EARG2

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610
ChainResidueDetails
ATHR3
ETHR3

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:11747826, ECO:0000269|PubMed:17194708
ChainResidueDetails
ELYS4
ALYS4

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: 5-glutamyl serotonin; alternate => ECO:0000269|PubMed:30867594
ChainResidueDetails
DLYS85
HLYS11
HLYS15
HLYS16
HLYS20
HLYS85
AGLN5
EGLN5
DLYS16
DLYS20

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by PKC => ECO:0000250|UniProtKB:P68431
ChainResidueDetails
BLYS44
ATHR6
ETHR6
FLYS8
FLYS16
FLYS44

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000269|PubMed:15485929
ChainResidueDetails
GLYS74
GLYS75
AARG8
EARG8

site_idSWS_FT_FI7
Number of Residues6
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:13678296, ECO:0000269|PubMed:17194708
ChainResidueDetails
ALYS36
ELYS9
ELYS27
ELYS36
ALYS9
ALYS27

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 => ECO:0000269|PubMed:10464286, ECO:0000269|PubMed:11856369, ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:15735677, ECO:0000269|PubMed:15870105
ChainResidueDetails
ASER10
ESER10
GLYS118
CLYS125
GLYS119
GLYS125

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by PKC and CHEK1 => ECO:0000250|UniProtKB:P68431
ChainResidueDetails
ATHR11
ETHR11
HLYS34
HLYS116

site_idSWS_FT_FI10
Number of Residues4
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P68431
ChainResidueDetails
ALYS14
ALYS122
ELYS14
ELYS122

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: Citrulline; alternate => ECO:0000269|PubMed:15339660
ChainResidueDetails
AARG17
EARG17
GLYS119

site_idSWS_FT_FI12
Number of Residues4
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:17194708
ChainResidueDetails
ELYS18
ALYS18
ALYS23
ELYS23

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: Citrulline => ECO:0000269|PubMed:15339660
ChainResidueDetails
AARG26
EARG26

site_idSWS_FT_FI14
Number of Residues2
DetailsMOD_RES: Phosphoserine; alternate; by AURKB, AURKC and RPS6KA5 => ECO:0000269|PubMed:10464286, ECO:0000269|PubMed:11441012, ECO:0000269|PubMed:11856369, ECO:0000269|PubMed:15684425, ECO:0000269|PubMed:15735677, ECO:0000269|PubMed:15870105
ChainResidueDetails
ESER28
ASER28

site_idSWS_FT_FI15
Number of Residues4
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000250|UniProtKB:P68431
ChainResidueDetails
FLYS12
FLYS20
FLYS59
FLYS79
ALYS37
ALYS64
ELYS37
ELYS64

site_idSWS_FT_FI16
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P68431
ChainResidueDetails
FLYS91
ETYR41
ATYR41

site_idSWS_FT_FI17
Number of Residues4
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435
ChainResidueDetails
ALYS56
ALYS79
ELYS56
ELYS79

site_idSWS_FT_FI18
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P68431
ChainResidueDetails
ASER57
ESER57

site_idSWS_FT_FI19
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P68431
ChainResidueDetails
ATHR80
ETHR80

site_idSWS_FT_FI20
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P84243
ChainResidueDetails
HLYS120
ASER86
ESER86

site_idSWS_FT_FI21
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ATHR107
ETHR107

site_idSWS_FT_FI22
Number of Residues2
DetailsMOD_RES: N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P68431
ChainResidueDetails
ALYS115
ELYS115

site_idSWS_FT_FI23
Number of Residues4
DetailsMOD_RES: Phosphoarginine => ECO:0000305
ChainResidueDetails
AARG128
AARG129
EARG128
EARG129

site_idSWS_FT_FI24
Number of Residues2
DetailsMOD_RES: Phosphoarginine => ECO:0000255
ChainResidueDetails
AARG131
EARG131

site_idSWS_FT_FI25
Number of Residues2
DetailsLIPID: N6-decanoyllysine => ECO:0000250|UniProtKB:P68431
ChainResidueDetails
ALYS18
ELYS18

218500

PDB entries from 2024-04-17

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