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4NFT

Crystal structure of human lnkH2B-h2A.Z-Anp32e

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
AALA103-VAL109

site_idPS00357
Number of Residues23
DetailsHISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG
ChainResidueDetails
AARG61-GLY83

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435
ChainResidueDetails
ALYS3
DLYS3
DLYS85
DLYS89
ALYS85
ALYS89
BLYS3
BLYS85
BLYS89
CLYS3
CLYS85
CLYS89

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: PolyADP-ribosyl glutamic acid => ECO:0000250|UniProtKB:Q64475
ChainResidueDetails
AGLU4
BGLU4
CGLU4
DGLU4

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphoserine; by AMPK => ECO:0000250|UniProtKB:Q64524
ChainResidueDetails
ASER5
BSER5
CSER5
DSER5

site_idSWS_FT_FI4
Number of Residues8
DetailsMOD_RES: N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732
ChainResidueDetails
ALYS12
ALYS54
BLYS12
BLYS54
CLYS12
CLYS54
DLYS12
DLYS54

site_idSWS_FT_FI5
Number of Residues8
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:16627869
ChainResidueDetails
ALYS15
ALYS77
BLYS15
BLYS77
CLYS15
CLYS77
DLYS15
DLYS77

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: N6-(2-hydroxyisobutyryl)lysine; alternate => ECO:0000269|PubMed:24681537
ChainResidueDetails
ALYS26
BLYS26
CLYS26
DLYS26

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: Dimethylated arginine => ECO:0000250|UniProtKB:Q96A08
ChainResidueDetails
AARG48
BARG48
CARG48
DARG48

site_idSWS_FT_FI8
Number of Residues8
DetailsMOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08
ChainResidueDetails
AARG55
AARG61
BARG55
BARG61
CARG55
CARG61
DARG55
DARG61

site_idSWS_FT_FI9
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q00729
ChainResidueDetails
ATHR84
BTHR84
CTHR84
DTHR84

site_idSWS_FT_FI10
Number of Residues4
DetailsCARBOHYD: O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807
ChainResidueDetails
ASER81
BSER81
CSER81
DSER81

site_idSWS_FT_FI11
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:21726816
ChainResidueDetails
ALYS3
BLYS3
CLYS3
DLYS3

site_idSWS_FT_FI12
Number of Residues8
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
ALYS89
BLYS89
CLYS89
DLYS89

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PDB entries from 2024-09-18

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