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7VCQ

structure of viral protein BKRF4 in complex with H3.3-H4-ASF1

Functional Information from GO Data
ChainGOidnamespacecontents
A0000786cellular_componentnucleosome
A0003677molecular_functionDNA binding
A0030527molecular_functionstructural constituent of chromatin
A0046982molecular_functionprotein heterodimerization activity
B0000781cellular_componentchromosome, telomeric region
B0000786cellular_componentnucleosome
B0003677molecular_functionDNA binding
B0003723molecular_functionRNA binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005694cellular_componentchromosome
B0006325biological_processchromatin organization
B0006334biological_processnucleosome assembly
B0016020cellular_componentmembrane
B0030527molecular_functionstructural constituent of chromatin
B0032200biological_processtelomere organization
B0032991cellular_componentprotein-containing complex
B0043505cellular_componentCENP-A containing nucleosome
B0045653biological_processnegative regulation of megakaryocyte differentiation
B0046982molecular_functionprotein heterodimerization activity
B0061644biological_processprotein localization to CENP-A containing chromatin
B0070062cellular_componentextracellular exosome
C0000786cellular_componentnucleosome
C0003677molecular_functionDNA binding
C0030527molecular_functionstructural constituent of chromatin
C0046982molecular_functionprotein heterodimerization activity
D0005634cellular_componentnucleus
D0006325biological_processchromatin organization
E0000781cellular_componentchromosome, telomeric region
E0000786cellular_componentnucleosome
E0003677molecular_functionDNA binding
E0003723molecular_functionRNA binding
E0005515molecular_functionprotein binding
E0005576cellular_componentextracellular region
E0005634cellular_componentnucleus
E0005654cellular_componentnucleoplasm
E0005694cellular_componentchromosome
E0006325biological_processchromatin organization
E0006334biological_processnucleosome assembly
E0016020cellular_componentmembrane
E0030527molecular_functionstructural constituent of chromatin
E0032200biological_processtelomere organization
E0032991cellular_componentprotein-containing complex
E0043505cellular_componentCENP-A containing nucleosome
E0045653biological_processnegative regulation of megakaryocyte differentiation
E0046982molecular_functionprotein heterodimerization activity
E0061644biological_processprotein localization to CENP-A containing chromatin
E0070062cellular_componentextracellular exosome
F0005634cellular_componentnucleus
F0006325biological_processchromatin organization
G0000786cellular_componentnucleosome
G0003677molecular_functionDNA binding
G0030527molecular_functionstructural constituent of chromatin
G0046982molecular_functionprotein heterodimerization activity
H0000781cellular_componentchromosome, telomeric region
H0000786cellular_componentnucleosome
H0003677molecular_functionDNA binding
H0003723molecular_functionRNA binding
H0005515molecular_functionprotein binding
H0005576cellular_componentextracellular region
H0005634cellular_componentnucleus
H0005654cellular_componentnucleoplasm
H0005694cellular_componentchromosome
H0006325biological_processchromatin organization
H0006334biological_processnucleosome assembly
H0016020cellular_componentmembrane
H0030527molecular_functionstructural constituent of chromatin
H0032200biological_processtelomere organization
H0032991cellular_componentprotein-containing complex
H0043505cellular_componentCENP-A containing nucleosome
H0045653biological_processnegative regulation of megakaryocyte differentiation
H0046982molecular_functionprotein heterodimerization activity
H0061644biological_processprotein localization to CENP-A containing chromatin
H0070062cellular_componentextracellular exosome
I0005634cellular_componentnucleus
I0006325biological_processchromatin organization
Functional Information from PROSITE/UniProt
site_idPS00047
Number of Residues5
DetailsHISTONE_H4 Histone H4 signature. GAKRH
ChainResidueDetails
BGLY14-HIS18

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 Residues12
DetailsDNA_BIND:
ChainResidueDetails
BLYS16-LYS20
ELYS16-LYS20
HLYS16-LYS20

site_idSWS_FT_FI2
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:17967882
ChainResidueDetails
BSER1
ESER1
HSER1

site_idSWS_FT_FI3
Number of Residues3
DetailsMOD_RES: Symmetric dimethylarginine; by PRMT5 and PRMT7; alternate => ECO:0000250|UniProtKB:P62806
ChainResidueDetails
BARG3
EARG3
HARG3

site_idSWS_FT_FI4
Number of Residues3
DetailsMOD_RES: N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732
ChainResidueDetails
BLYS5
ELYS5
HLYS5

site_idSWS_FT_FI5
Number of Residues9
DetailsMOD_RES: N6-propionyllysine; alternate => ECO:0000269|PubMed:17267393
ChainResidueDetails
BLYS8
BLYS16
BLYS44
ELYS8
ELYS16
ELYS44
HLYS8
HLYS16
HLYS44

site_idSWS_FT_FI6
Number of Residues12
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435
ChainResidueDetails
BLYS12
HLYS31
HLYS77
HLYS91
BLYS31
BLYS77
BLYS91
ELYS12
ELYS31
ELYS77
ELYS91
HLYS12

site_idSWS_FT_FI7
Number of Residues3
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:12086618, ECO:0000269|PubMed:15964846, ECO:0000269|PubMed:17967882, ECO:0000269|PubMed:27338793
ChainResidueDetails
BLYS20
ELYS20
HLYS20

site_idSWS_FT_FI8
Number of Residues3
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
BSER47
ESER47
HSER47

site_idSWS_FT_FI9
Number of Residues3
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455, ECO:0007744|PubMed:20068231
ChainResidueDetails
BTYR51
ETYR51
HTYR51

site_idSWS_FT_FI10
Number of Residues3
DetailsMOD_RES: N6-glutaryllysine; alternate => ECO:0000269|PubMed:31542297
ChainResidueDetails
BLYS59
ELYS59
HLYS59

site_idSWS_FT_FI11
Number of Residues3
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62806
ChainResidueDetails
BLYS79
ELYS79
HLYS79

site_idSWS_FT_FI12
Number of Residues3
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P62806
ChainResidueDetails
BTHR80
ETHR80
HTHR80

site_idSWS_FT_FI13
Number of Residues3
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:24275569
ChainResidueDetails
BTYR88
ETYR88
HTYR88

site_idSWS_FT_FI14
Number of Residues3
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25218447
ChainResidueDetails
BLYS12
ELYS12
HLYS12

site_idSWS_FT_FI15
Number of Residues6
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:19818714
ChainResidueDetails
BLYS91
ELYS91
HLYS91

site_idSWS_FT_FI16
Number of Residues9
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733
ChainResidueDetails
BLYS20
BLYS59
BLYS79
ELYS20
ELYS59
ELYS79
HLYS20
HLYS59
HLYS79

site_idSWS_FT_FI17
Number of Residues3
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate => ECO:0000269|PubMed:30886146
ChainResidueDetails
BLYS31
ELYS31
HLYS31

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PDB entries from 2024-11-06

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