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

7VDT

The motor-nucleosome module of human chromatin remodeling PBAF-nucleosome complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0006355biological_processregulation of DNA-templated transcription
A0042393molecular_functionhistone binding
B0000786cellular_componentnucleosome
B0003677molecular_functionDNA binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005694cellular_componentchromosome
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
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
K0003677molecular_functionDNA binding
K0005515molecular_functionprotein binding
K0005634cellular_componentnucleus
K0005654cellular_componentnucleoplasm
K0005694cellular_componentchromosome
K0030527molecular_functionstructural constituent of chromatin
K0046982molecular_functionprotein heterodimerization activity
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
ELYS14-LEU20

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

site_idPS00633
Number of Residues58
DetailsBROMODOMAIN_1 Bromodomain signature. SevFiqlpSrkelp..EYYelIrkpVdfkkIkerirnhk..Yrslndlekdvml.LcqNAqtF
ChainResidueDetails
ASER1449-PHE1506

site_idPS00959
Number of Residues9
DetailsHISTONE_H3_2 Histone H3 signature 2. PFqRLVREI
ChainResidueDetails
EPRO66-ILE74

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsMOD_RES: Citrulline; alternate => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
EARG2
EARG17
KARG2
KARG17
HLYS5
HLYS12
HLYS15
HLYS20

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by HASPIN and VRK1 => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ETHR3
KTHR3

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:12138181
ChainResidueDetails
ELYS4
KLYS4
GLYS9
GLYS95

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: 5-glutamyl serotonin; alternate => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
EGLN5
KGLN5
HLYS120

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: Phosphothreonine; by PKC => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ETHR6
ETHR11
KTHR6
KTHR11
FLYS8
FLYS16
FLYS44
FLYS79

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000250
ChainResidueDetails
EARG8
KARG8
FLYS12
FLYS20

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000305|PubMed:12138181
ChainResidueDetails
ELYS9
KLYS9
FLYS31
FLYS91

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ESER10
KSER10
CLYS15
CLYS119
GLYS13
GLYS15
GLYS119

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: N6-lactoyllysine; alternate => ECO:0000250|UniProtKB:P84228
ChainResidueDetails
ELYS14
KLYS14
FTYR51
FTYR88

site_idSWS_FT_FI10
Number of Residues10
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ELYS18
KLYS64
ELYS23
ELYS27
ELYS36
ELYS64
KLYS18
KLYS23
KLYS27
KLYS36

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: Citrulline => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
EARG26
KARG26

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: Phosphoserine; alternate; by AURKB, AURKC and RPS6KA5 => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ESER28
KSER28

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68431
ChainResidueDetails
ELYS37
KLYS37
FLYS91

site_idSWS_FT_FI14
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ETYR41
KTYR41

site_idSWS_FT_FI15
Number of Residues4
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228
ChainResidueDetails
ELYS56
ELYS79
KLYS56
KLYS79

site_idSWS_FT_FI16
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ESER57
KSER57

site_idSWS_FT_FI17
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ETHR80
ETHR107
KTHR80
KTHR107

site_idSWS_FT_FI18
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P84243
ChainResidueDetails
ESER86
KSER86

site_idSWS_FT_FI19
Number of Residues2
DetailsMOD_RES: N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ELYS115
KLYS115

site_idSWS_FT_FI20
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ELYS122
KLYS122

site_idSWS_FT_FI21
Number of Residues2
DetailsLIPID: S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ECYS110
KCYS110

227561

PDB entries from 2024-11-20

PDB statisticsPDBj update infoContact PDBjnumon