2NZD
Nucleosome core particle containing 145 bp of DNA
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 PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN E 1001 |
Chain | Residue |
D | VAL45 |
E | ASP77 |
E | HOH1008 |
E | HOH1010 |
E | HOH1012 |
F | HOH117 |
site_id | AC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE MN I 1003 |
Chain | Residue |
I | DG-34 |
I | DG-33 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE MN J 1004 |
Chain | Residue |
J | DG61 |
J | DG60 |
site_id | AC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE MN J 1005 |
Chain | Residue |
J | DG26 |
site_id | AC5 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE MN J 1006 |
Chain | Residue |
J | DG4 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MN J 1007 |
Chain | Residue |
J | DG47 |
J | HOH1015 |
J | HOH1019 |
site_id | AC7 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE MN I 1008 |
Chain | Residue |
I | DG47 |
site_id | AC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE MN I 1009 |
Chain | Residue |
I | DG60 |
I | HOH1013 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MN J 1010 |
Chain | Residue |
J | DG-34 |
J | DG-33 |
J | HOH1012 |
site_id | BC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE MN I 1011 |
Chain | Residue |
I | DA25 |
I | DG26 |
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 | PS00357 |
Number of Residues | 23 |
Details | HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG |
Chain | Residue | Details |
D | ARG89-GLY111 |
site_id | PS00959 |
Number of Residues | 9 |
Details | HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI |
Chain | Residue | Details |
A | PRO66-ILE74 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | MOD_RES: Citrulline; alternate => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | ARG2 | |
A | ARG17 | |
E | ARG2 | |
E | ARG17 | |
H | SER3 | |
H | GLY10 | |
H | LYS13 | |
H | THR18 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine; by HASPIN and VRK1 => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | THR3 | |
E | THR3 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:12138181 |
Chain | Residue | Details |
A | LYS4 | |
E | LYS4 | |
G | LYS9 | |
G | LYS95 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: 5-glutamyl serotonin; alternate => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | GLN5 | |
E | GLN5 | |
H | TYR118 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | MOD_RES: Phosphothreonine; by PKC => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | THR6 | |
A | THR11 | |
E | THR6 | |
E | THR11 | |
F | GLY9 | |
F | ARG17 | |
F | ARG45 | |
F | THR80 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000250 |
Chain | Residue | Details |
A | ARG8 | |
E | ARG8 | |
F | GLY13 | |
F | VAL21 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000305|PubMed:12138181 |
Chain | Residue | Details |
A | LYS9 | |
E | LYS9 | |
F | PRO32 | |
F | ARG92 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | SER10 | |
E | SER10 | |
C | LYS15 | |
C | LYS119 | |
G | LYS13 | |
G | LYS15 | |
G | LYS119 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | MOD_RES: N6-lactoyllysine; alternate => ECO:0000250|UniProtKB:P84228 |
Chain | Residue | Details |
A | LYS14 | |
E | LYS14 | |
F | GLU52 | |
F | ALA89 |
site_id | SWS_FT_FI10 |
Number of Residues | 10 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | LYS18 | |
E | LYS64 | |
A | LYS23 | |
A | LYS27 | |
A | LYS36 | |
A | LYS64 | |
E | LYS18 | |
E | LYS23 | |
E | LYS27 | |
E | LYS36 |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | MOD_RES: Citrulline => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | ARG26 | |
E | 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 |
A | SER28 | |
E | SER28 |
site_id | SWS_FT_FI13 |
Number of Residues | 2 |
Details | MOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68431 |
Chain | Residue | Details |
A | LYS37 | |
E | LYS37 | |
F | ARG92 |
site_id | SWS_FT_FI14 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | TYR41 | |
E | TYR41 |
site_id | SWS_FT_FI15 |
Number of Residues | 4 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 |
Chain | Residue | Details |
A | LYS56 | |
A | LYS79 | |
E | LYS56 | |
E | LYS79 |
site_id | SWS_FT_FI16 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | SER57 | |
E | SER57 |
site_id | SWS_FT_FI17 |
Number of Residues | 4 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | THR80 | |
A | THR107 | |
E | THR80 | |
E | THR107 |
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 |