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8I17

Structural basis for H2A-H2B recognitions by human Spt16

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
D0000786cellular_componentnucleosome
D0003677molecular_functionDNA binding
D0030527molecular_functionstructural constituent of chromatin
D0046982molecular_functionprotein heterodimerization activity
E0000786cellular_componentnucleosome
E0003677molecular_functionDNA binding
E0030527molecular_functionstructural constituent of chromatin
E0046982molecular_functionprotein heterodimerization activity
G0000786cellular_componentnucleosome
G0003677molecular_functionDNA binding
G0030527molecular_functionstructural constituent of chromatin
G0046982molecular_functionprotein heterodimerization activity
H0000786cellular_componentnucleosome
H0003677molecular_functionDNA binding
H0030527molecular_functionstructural constituent of chromatin
H0046982molecular_functionprotein heterodimerization activity
Functional Information from PROSITE/UniProt
site_idPS00046
Number of Residues7
DetailsHISTONE_H2A Histone H2A signature. AGLqFPV
ChainResidueDetails
AALA21-VAL27

site_idPS00357
Number of Residues23
DetailsHISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG
ChainResidueDetails
BARG92-GLY114

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues9
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435
ChainResidueDetails
BLYS34
BLYS116
BLYS120
ELYS34
ELYS116
ELYS120
HLYS34
HLYS116
HLYS120

site_idSWS_FT_FI2
Number of Residues3
DetailsMOD_RES: PolyADP-ribosyl glutamic acid => ECO:0000250|UniProtKB:Q64475
ChainResidueDetails
BGLU35
EGLU35
HGLU35

site_idSWS_FT_FI3
Number of Residues3
DetailsMOD_RES: Phosphoserine; by AMPK => ECO:0000250|UniProtKB:Q64475
ChainResidueDetails
BSER36
ESER36
HSER36
DLYS75
GLYS74
GLYS75

site_idSWS_FT_FI4
Number of Residues6
DetailsMOD_RES: N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732
ChainResidueDetails
BLYS43
BLYS85
ELYS43
ELYS85
HLYS43
HLYS85

site_idSWS_FT_FI5
Number of Residues6
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:16627869
ChainResidueDetails
BLYS46
BLYS108
ELYS46
ELYS108
HLYS46
HLYS108

site_idSWS_FT_FI6
Number of Residues3
DetailsMOD_RES: N6-(2-hydroxyisobutyryl)lysine; alternate => ECO:0000269|PubMed:24681537
ChainResidueDetails
BLYS57
ELYS57
HLYS57

site_idSWS_FT_FI7
Number of Residues3
DetailsMOD_RES: Dimethylated arginine => ECO:0000250|UniProtKB:Q96A08
ChainResidueDetails
BARG79
EARG79
HARG79
DLYS15
GLYS15

site_idSWS_FT_FI8
Number of Residues6
DetailsMOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08
ChainResidueDetails
BARG86
BARG92
EARG86
EARG92
HARG86
HARG92

site_idSWS_FT_FI9
Number of Residues3
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q00729
ChainResidueDetails
BTHR115
ETHR115
HTHR115

site_idSWS_FT_FI10
Number of Residues3
DetailsCARBOHYD: O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807
ChainResidueDetails
BSER112
ESER112
HSER112

site_idSWS_FT_FI11
Number of Residues3
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:21726816
ChainResidueDetails
BLYS34
ELYS34
HLYS34

site_idSWS_FT_FI12
Number of Residues6
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
BLYS120
ELYS120
HLYS120

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PDB entries from 2024-07-24

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