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3KUY

DNA Stretching in the Nucleosome Facilitates Alkylation by an Intercalating Antitumor Agent

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
A0046982molecular_functionprotein heterodimerization activity
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
Functional Information from PDB Data
site_id1
Number of Residues
Details
ChainResidue

site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MN E 1001
ChainResidue
DVAL45
EASP77

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ATV J 73
ChainResidue
IDC14
IDC15
JDG-15
JDG-14

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ATV I 73
ChainResidue
JDC15
IDG-15
IDG-14
JDC14

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 Residues8
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P0C1H4
ChainResidueDetails
DLYS2
DLYS9
DLYS12
DLYS17
HLYS2
HLYS9
HLYS12
HLYS17

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:12757711
ChainResidueDetails
DSER11
HSER11

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807
ChainResidueDetails
DSER109
HSER109
GLYS9
GLYS95

site_idSWS_FT_FI4
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0C1H4
ChainResidueDetails
DLYS117
GLYS36
HLYS117

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8
ChainResidueDetails
CLYS74
CLYS75
GLYS74
GLYS75
FLYS8
FLYS16
FLYS44
FLYS79

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N5-methylglutamine => ECO:0000250
ChainResidueDetails
CGLN104
GGLN104
FLYS12
FLYS20

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8
ChainResidueDetails
CLYS118
GLYS118
FLYS31
FLYS91

site_idSWS_FT_FI8
Number of Residues8
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250
ChainResidueDetails
CLYS13
FSER47
CLYS15
CLYS119
GLYS13
GLYS15
GLYS119

site_idSWS_FT_FI9
Number of Residues4
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P62805
ChainResidueDetails
BTYR51
BTYR88
FTYR51
FTYR88

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805
ChainResidueDetails
BLYS59
ELYS64
FLYS59
ALYS27
ALYS36
ALYS64
ELYS18
ELYS23
ELYS27
ELYS36

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P62805
ChainResidueDetails
BLYS77
FLYS77

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
BLYS31
FLYS31

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
ALYS37
BLYS91
FLYS91

site_idSWS_FT_FI14
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ATYR41
ETYR41

site_idSWS_FT_FI15
Number of Residues4
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228
ChainResidueDetails
ALYS56
ALYS79
ELYS56
ELYS79

site_idSWS_FT_FI16
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ASER57
ESER57

site_idSWS_FT_FI17
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ATHR80
ATHR107
ETHR80
ETHR107

site_idSWS_FT_FI18
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P84243
ChainResidueDetails
ASER86
ESER86

site_idSWS_FT_FI19
Number of Residues2
DetailsMOD_RES: N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ALYS115
ELYS115

site_idSWS_FT_FI20
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ALYS122
ELYS122

site_idSWS_FT_FI21
Number of Residues2
DetailsLIPID: S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ACYS110
ECYS110

227111

PDB entries from 2024-11-06

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