2FJ7
Crystal structure of Nucleosome Core Particle Containing a Poly (dA.dT) Sequence Element
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000786 | cellular_component | nucleosome |
A | 0003677 | molecular_function | DNA binding |
A | 0005515 | molecular_function | protein binding |
A | 0005634 | cellular_component | nucleus |
A | 0005654 | cellular_component | nucleoplasm |
A | 0005694 | cellular_component | chromosome |
A | 0030527 | molecular_function | structural constituent of chromatin |
A | 0046982 | molecular_function | protein heterodimerization activity |
B | 0000786 | cellular_component | nucleosome |
B | 0003677 | molecular_function | DNA binding |
B | 0005515 | molecular_function | protein binding |
B | 0005634 | cellular_component | nucleus |
B | 0005694 | cellular_component | chromosome |
B | 0006334 | biological_process | nucleosome assembly |
B | 0030527 | molecular_function | structural constituent of chromatin |
B | 0046982 | molecular_function | protein heterodimerization activity |
C | 0000786 | cellular_component | nucleosome |
C | 0003677 | molecular_function | DNA binding |
C | 0005634 | cellular_component | nucleus |
C | 0005694 | cellular_component | chromosome |
C | 0030527 | molecular_function | structural constituent of chromatin |
C | 0046982 | molecular_function | protein heterodimerization activity |
D | 0000786 | cellular_component | nucleosome |
D | 0003677 | molecular_function | DNA binding |
D | 0005515 | molecular_function | protein binding |
D | 0005634 | cellular_component | nucleus |
D | 0005694 | cellular_component | chromosome |
D | 0030527 | molecular_function | structural constituent of chromatin |
D | 0046982 | molecular_function | protein heterodimerization activity |
E | 0000786 | cellular_component | nucleosome |
E | 0003677 | molecular_function | DNA binding |
E | 0005515 | molecular_function | protein binding |
E | 0005634 | cellular_component | nucleus |
E | 0005654 | cellular_component | nucleoplasm |
E | 0005694 | cellular_component | chromosome |
E | 0030527 | molecular_function | structural constituent of chromatin |
E | 0046982 | molecular_function | protein heterodimerization activity |
F | 0000786 | cellular_component | nucleosome |
F | 0003677 | molecular_function | DNA binding |
F | 0005515 | molecular_function | protein binding |
F | 0005634 | cellular_component | nucleus |
F | 0005694 | cellular_component | chromosome |
F | 0006334 | biological_process | nucleosome assembly |
F | 0030527 | molecular_function | structural constituent of chromatin |
F | 0046982 | molecular_function | protein heterodimerization activity |
G | 0000786 | cellular_component | nucleosome |
G | 0003677 | molecular_function | DNA binding |
G | 0005634 | cellular_component | nucleus |
G | 0005694 | cellular_component | chromosome |
G | 0030527 | molecular_function | structural constituent of chromatin |
G | 0046982 | molecular_function | protein heterodimerization activity |
H | 0000786 | cellular_component | nucleosome |
H | 0003677 | molecular_function | DNA binding |
H | 0005515 | molecular_function | protein binding |
H | 0005634 | cellular_component | nucleus |
H | 0005694 | cellular_component | chromosome |
H | 0030527 | molecular_function | structural constituent of chromatin |
H | 0046982 | molecular_function | protein heterodimerization activity |
Functional Information from PROSITE/UniProt
site_id | PS00046 |
Number of Residues | 7 |
Details | HISTONE_H2A Histone H2A signature. AGLqFPV |
Chain | Residue | Details |
C | ALA21-VAL27 |
site_id | PS00047 |
Number of Residues | 5 |
Details | HISTONE_H4 Histone H4 signature. GAKRH |
Chain | Residue | Details |
B | GLY14-HIS18 |
site_id | PS00322 |
Number of Residues | 7 |
Details | HISTONE_H3_1 Histone H3 signature 1. KAPRKQL |
Chain | Residue | Details |
A | LYS14-LEU20 |
site_id | PS00959 |
Number of Residues | 9 |
Details | HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI |
Chain | Residue | Details |
A | PRO66-ILE74 |
site_id | PS00357 |
Number of Residues | 23 |
Details | HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG |
Chain | Residue | Details |
D | ARG89-GLY111 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250 |
Chain | Residue | Details |
C | SER1 | |
G | SER1 | |
E | ARG2 | |
E | ARG17 | |
H | SER3 | |
H | GLY10 | |
H | LYS13 | |
H | THR18 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250 |
Chain | Residue | Details |
C | LYS5 | |
G | LYS5 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P0C0S8 |
Chain | Residue | Details |
C | LYS9 | |
C | LYS95 | |
G | LYS9 | |
G | LYS95 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: N6-(2-hydroxyisobutyryl)lysine; alternate => ECO:0000250|UniProtKB:P0C0S8 |
Chain | Residue | Details |
C | LYS36 | |
G | LYS36 | |
H | TYR118 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 |
Chain | Residue | Details |
C | LYS74 | |
C | LYS75 | |
G | LYS74 | |
G | LYS75 | |
F | GLY9 | |
F | ARG17 | |
F | ARG45 | |
F | THR80 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: N5-methylglutamine => ECO:0000250 |
Chain | Residue | Details |
C | GLN104 | |
G | GLN104 | |
F | GLY13 | |
F | VAL21 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8 |
Chain | Residue | Details |
C | LYS118 | |
G | LYS118 | |
F | PRO32 | |
F | ARG92 |
site_id | SWS_FT_FI8 |
Number of Residues | 8 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250 |
Chain | Residue | Details |
C | LYS13 | |
E | SER10 | |
G | LYS15 | |
G | LYS119 | |
C | LYS15 | |
C | LYS119 | |
G | LYS13 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | MOD_RES: N6-lactoyllysine; alternate => ECO:0000250|UniProtKB:P84228 |
Chain | Residue | Details |
F | GLU52 | |
F | ALA89 | |
A | LYS14 | |
E | LYS14 |
site_id | SWS_FT_FI10 |
Number of Residues | 10 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | LYS23 | |
A | LYS27 | |
A | LYS36 | |
A | LYS64 | |
E | LYS18 | |
E | LYS23 | |
E | LYS27 | |
E | LYS36 | |
E | LYS64 | |
A | LYS18 |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | MOD_RES: Citrulline => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
E | ARG26 | |
A | ARG26 |
site_id | SWS_FT_FI12 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine; alternate; by AURKB, AURKC and RPS6KA5 => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
E | SER28 | |
A | SER28 |
site_id | SWS_FT_FI13 |
Number of Residues | 2 |
Details | MOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68431 |
Chain | Residue | Details |
E | LYS37 | |
A | LYS37 | |
F | ARG92 |
site_id | SWS_FT_FI14 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
E | TYR41 | |
A | TYR41 |
site_id | SWS_FT_FI15 |
Number of Residues | 4 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 |
Chain | Residue | Details |
E | LYS56 | |
E | LYS79 | |
A | LYS56 | |
A | LYS79 |
site_id | SWS_FT_FI16 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
E | SER57 | |
A | SER57 |
site_id | SWS_FT_FI17 |
Number of Residues | 4 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
E | THR80 | |
E | THR107 | |
A | THR107 | |
A | THR80 |
site_id | SWS_FT_FI18 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P84243 |
Chain | Residue | Details |
A | SER86 | |
E | SER86 |
site_id | SWS_FT_FI19 |
Number of Residues | 2 |
Details | MOD_RES: N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | LYS115 | |
E | LYS115 |
site_id | SWS_FT_FI20 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | LYS122 | |
E | LYS122 |
site_id | SWS_FT_FI21 |
Number of Residues | 2 |
Details | LIPID: S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | CYS110 | |
E | CYS110 |