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

1TZY

Crystal Structure of the Core-Histone Octamer to 1.90 Angstrom Resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0000786cellular_componentnucleosome
A0003677molecular_functionDNA binding
A0005634cellular_componentnucleus
A0005694cellular_componentchromosome
A0030527molecular_functionstructural constituent of chromatin
A0031492molecular_functionnucleosomal DNA binding
A0031507biological_processheterochromatin formation
A0046982molecular_functionprotein heterodimerization activity
B0000786cellular_componentnucleosome
B0003677molecular_functionDNA binding
B0005634cellular_componentnucleus
B0005694cellular_componentchromosome
B0030527molecular_functionstructural constituent of chromatin
B0044877molecular_functionprotein-containing complex binding
B0046982molecular_functionprotein heterodimerization activity
C0000122biological_processnegative regulation of transcription by RNA polymerase II
C0000785cellular_componentchromatin
C0000786cellular_componentnucleosome
C0003677molecular_functionDNA binding
C0003682molecular_functionchromatin binding
C0005634cellular_componentnucleus
C0005694cellular_componentchromosome
C0010467biological_processgene expression
C0030527molecular_functionstructural constituent of chromatin
C0046982molecular_functionprotein heterodimerization activity
D0000786cellular_componentnucleosome
D0003677molecular_functionDNA binding
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005694cellular_componentchromosome
D0006334biological_processnucleosome assembly
D0030527molecular_functionstructural constituent of chromatin
D0046982molecular_functionprotein heterodimerization activity
E0000786cellular_componentnucleosome
E0003677molecular_functionDNA binding
E0005634cellular_componentnucleus
E0005694cellular_componentchromosome
E0030527molecular_functionstructural constituent of chromatin
E0031492molecular_functionnucleosomal DNA binding
E0031507biological_processheterochromatin formation
E0046982molecular_functionprotein heterodimerization activity
F0000786cellular_componentnucleosome
F0003677molecular_functionDNA binding
F0005634cellular_componentnucleus
F0005694cellular_componentchromosome
F0030527molecular_functionstructural constituent of chromatin
F0044877molecular_functionprotein-containing complex binding
F0046982molecular_functionprotein heterodimerization activity
G0000122biological_processnegative regulation of transcription by RNA polymerase II
G0000785cellular_componentchromatin
G0000786cellular_componentnucleosome
G0003677molecular_functionDNA binding
G0003682molecular_functionchromatin binding
G0005634cellular_componentnucleus
G0005694cellular_componentchromosome
G0010467biological_processgene expression
G0030527molecular_functionstructural constituent of chromatin
G0046982molecular_functionprotein heterodimerization activity
H0000786cellular_componentnucleosome
H0003677molecular_functionDNA binding
H0005634cellular_componentnucleus
H0005654cellular_componentnucleoplasm
H0005694cellular_componentchromosome
H0006334biological_processnucleosome assembly
H0030527molecular_functionstructural constituent of chromatin
H0046982molecular_functionprotein heterodimerization activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A 1501
ChainResidue
AARG29
AARG32
ALYS36
AHOH1697
AHOH1705
DLYS31

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 B 1502
ChainResidue
BLYS57
AILE79
APRO80
BSER55

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 E 1503
ChainResidue
EARG29
EARG32
ELYS36

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 E 1504
ChainResidue
EARG77
EHOH1704
FSER55
FSER56

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 C 1505
ChainResidue
CARG49
CGLU50
CARG53
CHOH1675

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL G 1601
ChainResidue
GLEU60
GLYS64

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL E 1602
ChainResidue
EGLY44
EGLY46
EALA47
FTHR90
FSER91

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL D 1603
ChainResidue
DARG39
DARG45
DILE46
DHOH1683

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 1604
ChainResidue
AARG35
AHOH1627
DLYS31

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL H 1605
ChainResidue
ATHR101
GALA95
HARG95

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL B 1606
ChainResidue
AGLY44
AGLY46
AALA47
BTHR90
BSER91

site_idBC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL C 1607
ChainResidue
CLYS122

site_idBC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL G 1608
ChainResidue
GLYS122

site_idBC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL G 1609
ChainResidue
GARG116
GVAL117
GTHR118

site_idBC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL H 1610
ChainResidue
HARG35
HARG39
HARG45
HILE46

site_idBC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL G 1611
ChainResidue
FHOH1687
GGLN68
GARG69
GARG72
GHOH1637

site_idBC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL D 1612
ChainResidue
DTHR30
DHOH1654

site_idBC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 1613
ChainResidue
ALEU85
AASN89

site_idCC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 1614
ChainResidue
BSER64
HGLY101

site_idCC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL C 1615
ChainResidue
CVAL117
CTHR118

site_idCC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL F 1616
ChainResidue
FLYS116
HLEU22
HARG23
HASN25

site_idCC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL D 1617
ChainResidue
CALA95
DARG95
ETHR101

site_idCC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL H 1618
ChainResidue
HTHR30
HLYS31

site_idCC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL C 1619
ChainResidue
CGLN125
CARG128
DHOH1663

site_idCC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 1620
ChainResidue
AILE111

site_idCC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL E 1621
ChainResidue
EARG17
ESER18
EVAL27
EGLY28

site_idCC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 1622
ChainResidue
AARG29
DLYS31

site_idDC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL F 1623
ChainResidue
FSER64

Functional Information from PROSITE/UniProt
site_idPS00046
Number of Residues7
DetailsHISTONE_H2A Histone H2A signature. AGLqFPV
ChainResidueDetails
AALA21-VAL27

site_idPS00047
Number of Residues5
DetailsHISTONE_H4 Histone H4 signature. GAKRH
ChainResidueDetails
DGLY14-HIS18

site_idPS00322
Number of Residues7
DetailsHISTONE_H3_1 Histone H3 signature 1. KAPRKQL
ChainResidueDetails
CLYS14-LEU20

site_idPS00357
Number of Residues23
DetailsHISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG
ChainResidueDetails
BARG92-GLY114

site_idPS00959
Number of Residues9
DetailsHISTONE_H3_2 Histone H3 signature 2. PFqRLVREI
ChainResidueDetails
CPRO66-ILE74

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsDNA_BIND:
ChainResidueDetails
DLYS16-LYS20
HLYS16-LYS20
BLYS16
BTHR21
FSER6
FGLY13
FLYS16
FTHR21

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P62805
ChainResidueDetails
DSER1
HSER1
GARG2
GARG17

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Symmetric dimethylarginine; by PRMT5 and PRMT7; alternate => ECO:0000250|UniProtKB:P62805
ChainResidueDetails
DARG3
HARG3
EALA10
ELEU96

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-lactoyllysine; alternate => ECO:0000250|UniProtKB:P62805
ChainResidueDetails
DLYS5
HLYS5
FTYR121

site_idSWS_FT_FI5
Number of Residues8
DetailsMOD_RES: N6-propionyllysine; alternate => ECO:0000250|UniProtKB:P62805
ChainResidueDetails
DLYS8
DLYS16
DLYS44
DLYS79
HLYS8
HLYS16
HLYS44
HLYS79

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000250|UniProtKB:P62805
ChainResidueDetails
DLYS12
DLYS20
HLYS12
HLYS20

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62805
ChainResidueDetails
DLYS31
DLYS91
HLYS31
HLYS91

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PAK2 => ECO:0000250|UniProtKB:P62805
ChainResidueDetails
DSER47
HSER47
ELYS119
ETHR120

site_idSWS_FT_FI9
Number of Residues4
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P62805
ChainResidueDetails
DTYR51
DTYR88
HTYR51
HTYR88

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805
ChainResidueDetails
DLYS59
HLYS59
ETHR120

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P62805
ChainResidueDetails
DLYS77
HLYS77
CLYS64
GLYS18
GLYS23
GLYS64

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
DLYS31
HLYS31

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
CLYS27
DLYS91
GLYS27
HLYS91

site_idSWS_FT_FI14
Number of Residues2
DetailsMOD_RES: Phosphoserine; alternate; by AURKB, AURKC and RPS6KA5 => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
CSER28
GSER28

site_idSWS_FT_FI15
Number of Residues2
DetailsMOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68431
ChainResidueDetails
CLYS37
GLYS37

site_idSWS_FT_FI16
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
CTYR41
GTYR41

site_idSWS_FT_FI17
Number of Residues4
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228
ChainResidueDetails
CLYS56
CLYS79
GLYS56
GLYS79

site_idSWS_FT_FI18
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
CSER57
GSER57

site_idSWS_FT_FI19
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
CTHR80
CTHR107
GTHR80
GTHR107

site_idSWS_FT_FI20
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P84243
ChainResidueDetails
CSER86
GSER86

site_idSWS_FT_FI21
Number of Residues2
DetailsMOD_RES: N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
CLYS115
GLYS115

site_idSWS_FT_FI22
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
CLYS122
GLYS122

site_idSWS_FT_FI23
Number of Residues2
DetailsLIPID: S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
CCYS110
GCYS110

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon