Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

8OOS

CryoEM Structure INO80core Hexasome complex ATPase-hexasome refinement state 2

Functional Information from GO Data
ChainGOidnamespacecontents
G0003677molecular_functionDNA binding
G0005524molecular_functionATP binding
G0005634cellular_componentnucleus
G0006281biological_processDNA repair
G0006338biological_processchromatin remodeling
G0006351biological_processDNA-templated transcription
G0031011cellular_componentIno80 complex
G0140658molecular_functionATP-dependent chromatin remodeler activity
M0000786cellular_componentnucleosome
M0003677molecular_functionDNA binding
M0005515molecular_functionprotein binding
M0005576cellular_componentextracellular region
M0005634cellular_componentnucleus
M0005654cellular_componentnucleoplasm
M0005694cellular_componentchromosome
M0006325biological_processchromatin organization
M0006334biological_processnucleosome assembly
M0010467biological_processgene expression
M0016020cellular_componentmembrane
M0030527molecular_functionstructural constituent of chromatin
M0032200biological_processtelomere organization
M0032991cellular_componentprotein-containing complex
M0040029biological_processepigenetic regulation of gene expression
M0045296molecular_functioncadherin binding
M0046982molecular_functionprotein heterodimerization activity
M0070062cellular_componentextracellular exosome
N0000781cellular_componentchromosome, telomeric region
N0000786cellular_componentnucleosome
N0003677molecular_functionDNA binding
N0003723molecular_functionRNA binding
N0005515molecular_functionprotein binding
N0005576cellular_componentextracellular region
N0005634cellular_componentnucleus
N0005654cellular_componentnucleoplasm
N0005694cellular_componentchromosome
N0006325biological_processchromatin organization
N0006334biological_processnucleosome assembly
N0016020cellular_componentmembrane
N0030527molecular_functionstructural constituent of chromatin
N0032200biological_processtelomere organization
N0032991cellular_componentprotein-containing complex
N0043505cellular_componentCENP-A containing nucleosome
N0045653biological_processnegative regulation of megakaryocyte differentiation
N0046982molecular_functionprotein heterodimerization activity
N0061644biological_processprotein localization to CENP-A containing chromatin
N0070062cellular_componentextracellular exosome
O0000786cellular_componentnucleosome
O0003677molecular_functionDNA binding
O0005515molecular_functionprotein binding
O0005634cellular_componentnucleus
O0005654cellular_componentnucleoplasm
O0005694cellular_componentchromosome
O0008285biological_processnegative regulation of cell population proliferation
O0030527molecular_functionstructural constituent of chromatin
O0031507biological_processheterochromatin formation
O0046982molecular_functionprotein heterodimerization activity
O0070062cellular_componentextracellular exosome
P0000786cellular_componentnucleosome
P0002227biological_processinnate immune response in mucosa
P0003677molecular_functionDNA binding
P0005515molecular_functionprotein binding
P0005615cellular_componentextracellular space
P0005634cellular_componentnucleus
P0005654cellular_componentnucleoplasm
P0005694cellular_componentchromosome
P0005829cellular_componentcytosol
P0006334biological_processnucleosome assembly
P0019731biological_processantibacterial humoral response
P0030527molecular_functionstructural constituent of chromatin
P0042742biological_processdefense response to bacterium
P0042802molecular_functionidentical protein binding
P0046982molecular_functionprotein heterodimerization activity
P0050830biological_processdefense response to Gram-positive bacterium
P0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
P0070062cellular_componentextracellular exosome
Q0000786cellular_componentnucleosome
Q0003677molecular_functionDNA binding
Q0005515molecular_functionprotein binding
Q0005576cellular_componentextracellular region
Q0005634cellular_componentnucleus
Q0005654cellular_componentnucleoplasm
Q0005694cellular_componentchromosome
Q0006325biological_processchromatin organization
Q0006334biological_processnucleosome assembly
Q0010467biological_processgene expression
Q0016020cellular_componentmembrane
Q0030527molecular_functionstructural constituent of chromatin
Q0032200biological_processtelomere organization
Q0032991cellular_componentprotein-containing complex
Q0040029biological_processepigenetic regulation of gene expression
Q0045296molecular_functioncadherin binding
Q0046982molecular_functionprotein heterodimerization activity
Q0070062cellular_componentextracellular exosome
R0000781cellular_componentchromosome, telomeric region
R0000786cellular_componentnucleosome
R0003677molecular_functionDNA binding
R0003723molecular_functionRNA binding
R0005515molecular_functionprotein binding
R0005576cellular_componentextracellular region
R0005634cellular_componentnucleus
R0005654cellular_componentnucleoplasm
R0005694cellular_componentchromosome
R0006325biological_processchromatin organization
R0006334biological_processnucleosome assembly
R0016020cellular_componentmembrane
R0030527molecular_functionstructural constituent of chromatin
R0032200biological_processtelomere organization
R0032991cellular_componentprotein-containing complex
R0043505cellular_componentCENP-A containing nucleosome
R0045653biological_processnegative regulation of megakaryocyte differentiation
R0046982molecular_functionprotein heterodimerization activity
R0061644biological_processprotein localization to CENP-A containing chromatin
R0070062cellular_componentextracellular exosome
Functional Information from PROSITE/UniProt
site_idPS00046
Number of Residues7
DetailsHISTONE_H2A Histone H2A signature. AGLqFPV
ChainResidueDetails
OALA21-VAL27

site_idPS00047
Number of Residues5
DetailsHISTONE_H4 Histone H4 signature. GAKRH
ChainResidueDetails
NGLY14-HIS18

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

site_idPS00357
Number of Residues23
DetailsHISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG
ChainResidueDetails
PARG89-GLY111

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsDNA_BIND:
ChainResidueDetails
NLYS16-LYS20
RLYS16-LYS20

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:17967882
ChainResidueDetails
NSER1
RSER1

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Symmetric dimethylarginine; by PRMT5 and PRMT7; alternate => ECO:0000250|UniProtKB:P62806
ChainResidueDetails
NARG3
RARG3
PLYS12
PLYS13
PLYS17
PLYS20
PLYS40
PLYS82

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732
ChainResidueDetails
NLYS5
RLYS5

site_idSWS_FT_FI5
Number of Residues6
DetailsMOD_RES: N6-propionyllysine; alternate => ECO:0000269|PubMed:17267393
ChainResidueDetails
NLYS8
NLYS16
NLYS44
RLYS8
RLYS16
RLYS44

site_idSWS_FT_FI6
Number of Residues8
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435
ChainResidueDetails
NLYS12
NLYS31
NLYS77
NLYS91
RLYS12
RLYS31
RLYS77
RLYS91

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:12086618, ECO:0000269|PubMed:15964846, ECO:0000269|PubMed:17967882, ECO:0000269|PubMed:27338793
ChainResidueDetails
NLYS20
RLYS20

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PAK2 => ECO:0000269|PubMed:21724829, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
NSER47
RSER47
PLYS117

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455, ECO:0007744|PubMed:20068231
ChainResidueDetails
NTYR51
RTYR51
OLYS125

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: N6-glutaryllysine; alternate => ECO:0000269|PubMed:31542297
ChainResidueDetails
NLYS59
RLYS59
QLYS14
QLYS56

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62806
ChainResidueDetails
NLYS79
RLYS79

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P62806
ChainResidueDetails
NTHR80
RTHR80
QLYS18
QLYS64

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:24275569
ChainResidueDetails
NTYR88
RTYR88

site_idSWS_FT_FI14
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25218447
ChainResidueDetails
NLYS12
RLYS12

site_idSWS_FT_FI15
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:19818714
ChainResidueDetails
MLYS27
NLYS91
RLYS91

site_idSWS_FT_FI16
Number of Residues6
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733
ChainResidueDetails
NLYS20
NLYS59
NLYS79
RLYS20
RLYS59
RLYS79

site_idSWS_FT_FI17
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate => ECO:0000269|PubMed:30886146
ChainResidueDetails
NLYS31
RLYS31

site_idSWS_FT_FI18
Number of Residues2
DetailsMOD_RES: N6-methyllysine => ECO:0000269|PubMed:15983376
ChainResidueDetails
MLYS37
QLYS37

site_idSWS_FT_FI19
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:19783980
ChainResidueDetails
MTYR41
QTYR41

site_idSWS_FT_FI20
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:20850016
ChainResidueDetails
MSER57
QSER57

site_idSWS_FT_FI21
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435, ECO:0000269|PubMed:29211711
ChainResidueDetails
MLYS79
QLYS79

site_idSWS_FT_FI22
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:20850016
ChainResidueDetails
MTHR80
QTHR80

site_idSWS_FT_FI23
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P84243
ChainResidueDetails
MSER86
QSER86

site_idSWS_FT_FI24
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
MTHR107
QTHR107

site_idSWS_FT_FI25
Number of Residues2
DetailsMOD_RES: N6-glutaryllysine; alternate => ECO:0000269|PubMed:31542297
ChainResidueDetails
MLYS115
QLYS115

site_idSWS_FT_FI26
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435, ECO:0000269|PubMed:27436229
ChainResidueDetails
MLYS122
QLYS122

site_idSWS_FT_FI27
Number of Residues2
DetailsLIPID: N6-decanoyllysine => ECO:0000269|PubMed:35939806
ChainResidueDetails
MLYS18
QLYS18

237423

PDB entries from 2025-06-11

PDB statisticsPDBj update infoContact PDBjnumon