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

6KBB

Role of the DEF/Y motif of Swc5 in histone H2A.Z deposition

Functional Information from GO Data
ChainGOidnamespacecontents
A0000786cellular_componentnucleosome
A0003677molecular_functionDNA binding
A0030527molecular_functionstructural constituent of chromatin
A0046982molecular_functionprotein heterodimerization activity
B0000786cellular_componentnucleosome
B0003677molecular_functionDNA binding
B0030527molecular_functionstructural constituent of chromatin
B0046982molecular_functionprotein heterodimerization activity
C0000786cellular_componentnucleosome
C0003677molecular_functionDNA binding
C0030527molecular_functionstructural constituent of chromatin
C0046982molecular_functionprotein heterodimerization activity
D0000786cellular_componentnucleosome
D0003677molecular_functionDNA binding
D0030527molecular_functionstructural constituent of chromatin
D0046982molecular_functionprotein heterodimerization activity
Functional Information from PROSITE/UniProt
site_idPS00046
Number of Residues7
DetailsHISTONE_H2A Histone H2A signature. AGLqFPV
ChainResidueDetails
CALA21-VAL27

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435
ChainResidueDetails
DLYS34
DLYS116
DLYS120
BLYS34
BLYS116
BLYS120

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: PolyADP-ribosyl glutamic acid => ECO:0000250|UniProtKB:Q64475
ChainResidueDetails
DGLU35
BGLU35

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine; by AMPK => ECO:0000250|UniProtKB:Q64524
ChainResidueDetails
DSER36
BSER36
ALYS74
ALYS75

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732
ChainResidueDetails
DLYS43
DLYS85
BLYS43
BLYS85

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:16627869
ChainResidueDetails
DLYS46
DLYS108
BLYS46
BLYS108

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-(2-hydroxyisobutyryl)lysine; alternate => ECO:0000269|PubMed:24681537
ChainResidueDetails
DLYS57
BLYS57

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Dimethylated arginine => ECO:0000250|UniProtKB:Q96A08
ChainResidueDetails
DARG79
BARG79

site_idSWS_FT_FI8
Number of Residues4
DetailsMOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08
ChainResidueDetails
DARG86
DARG92
BARG86
BARG92

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q00729
ChainResidueDetails
DTHR115
BTHR115

site_idSWS_FT_FI10
Number of Residues2
DetailsCARBOHYD: O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807
ChainResidueDetails
DSER112
BSER112

site_idSWS_FT_FI11
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:21726816
ChainResidueDetails
DLYS34
BLYS34

site_idSWS_FT_FI12
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:16307923, ECO:0000269|PubMed:16627869, ECO:0000269|PubMed:16713563
ChainResidueDetails
DLYS120
BLYS120

223166

PDB entries from 2024-07-31

PDB statisticsPDBj update infoContact PDBjnumon