6R25
Structure of LSD2/NPAC-linker/nucleosome core particle complex: Class 3
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 |
K | 0000786 | cellular_component | nucleosome |
K | 0003682 | molecular_function | chromatin binding |
K | 0005515 | molecular_function | protein binding |
K | 0005634 | cellular_component | nucleus |
K | 0005654 | cellular_component | nucleoplasm |
K | 0005694 | cellular_component | chromosome |
K | 0006325 | biological_process | chromatin organization |
K | 0006338 | biological_process | chromatin remodeling |
K | 0008270 | molecular_function | zinc ion binding |
K | 0016491 | molecular_function | oxidoreductase activity |
K | 0032452 | molecular_function | histone demethylase activity |
K | 0032453 | molecular_function | histone H3K4 demethylase activity |
K | 0042393 | molecular_function | histone binding |
K | 0044726 | biological_process | epigenetic programing of female pronucleus |
K | 0046872 | molecular_function | metal ion binding |
K | 0050660 | molecular_function | flavin adenine dinucleotide binding |
K | 0071514 | biological_process | genomic imprinting |
K | 0071949 | molecular_function | FAD binding |
K | 0140682 | molecular_function | FAD-dependent H3K4me/H3K4me3 demethylase activity |
M | 0000786 | cellular_component | nucleosome |
M | 0003677 | molecular_function | DNA binding |
M | 0005515 | molecular_function | protein binding |
M | 0005634 | cellular_component | nucleus |
M | 0005654 | cellular_component | nucleoplasm |
M | 0005694 | cellular_component | chromosome |
M | 0030527 | molecular_function | structural constituent of chromatin |
M | 0046982 | molecular_function | protein heterodimerization activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 32 |
Details | binding site for residue FAD K 901 |
Chain | Residue |
K | ILE388 |
K | GLY419 |
K | ARG420 |
K | ARG434 |
K | GLY435 |
K | ALA436 |
K | ILE438 |
K | VAL598 |
K | VAL627 |
K | PRO628 |
K | TRP757 |
K | GLY389 |
K | TRP762 |
K | ALA766 |
K | GLY794 |
K | GLU795 |
K | GLN803 |
K | THR804 |
K | VAL805 |
K | ALA808 |
K | HOH1058 |
K | HOH1062 |
K | GLY391 |
K | HOH1119 |
K | HOH1125 |
K | HOH1128 |
K | PRO392 |
K | ALA393 |
K | LEU411 |
K | GLU412 |
K | ALA413 |
K | LYS414 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue ZN K 902 |
Chain | Residue |
K | CYS53 |
K | CYS58 |
K | HIS84 |
K | HIS90 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue ZN K 903 |
Chain | Residue |
K | CYS65 |
K | CYS73 |
K | CYS92 |
K | CYS95 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue ZN K 904 |
Chain | Residue |
K | CYS142 |
K | CYS147 |
K | CYS169 |
K | CYS185 |
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 |
M | LYS14-LEU20 | |
A | LYS14-LEU20 |
site_id | PS00959 |
Number of Residues | 9 |
Details | HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI |
Chain | Residue | Details |
M | PRO66-ILE74 | |
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: Citrulline; alternate => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
M | ARG2 | |
M | ARG17 | |
D | LYS12 | |
D | LYS17 | |
H | LYS2 | |
H | LYS9 | |
H | LYS12 | |
H | LYS17 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine; by HASPIN => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
K | CYS65 | |
K | CYS73 | |
K | HIS84 | |
K | HIS90 | |
K | CYS92 | |
K | CYS95 | |
K | VAL598 | |
K | GLN803 | |
M | THR3 | |
H | SER11 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:12138181 |
Chain | Residue | Details |
H | SER109 | |
G | LYS9 | |
G | LYS95 | |
M | MET4 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: 5-glutamyl serotonin; alternate => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
G | LYS36 | |
H | LYS117 | |
M | GLN5 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine; by PKC => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
M | THR6 | |
M | THR11 | |
G | LYS74 | |
G | LYS75 | |
F | LYS8 | |
F | LYS16 | |
F | LYS44 | |
F | LYS79 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000250 |
Chain | Residue | Details |
M | ARG8 | |
G | GLN104 | |
F | LYS12 | |
F | LYS20 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000305|PubMed:12138181 |
Chain | Residue | Details |
M | LYS9 | |
G | LYS118 | |
F | LYS31 | |
F | LYS91 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
G | LYS15 | |
G | LYS119 | |
M | SER10 | |
F | SER47 | |
C | LYS15 | |
C | LYS119 | |
G | LYS13 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | MOD_RES: N6-lactoyllysine; alternate => ECO:0000250|UniProtKB:P84228 |
Chain | Residue | Details |
M | LYS14 | |
B | TYR88 | |
F | TYR51 | |
F | TYR88 |
site_id | SWS_FT_FI10 |
Number of Residues | 5 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
M | LYS27 | |
M | LYS36 | |
M | LYS64 | |
E | LYS18 | |
E | LYS23 | |
E | LYS27 | |
E | LYS36 | |
E | LYS64 | |
M | LYS18 | |
M | LYS23 |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | MOD_RES: Citrulline => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
M | ARG26 | |
F | LYS77 |
site_id | SWS_FT_FI12 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; alternate; by AURKB, AURKC and RPS6KA5 => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
M | SER28 | |
F | LYS31 |
site_id | SWS_FT_FI13 |
Number of Residues | 1 |
Details | MOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68431 |
Chain | Residue | Details |
M | LYS37 | |
B | LYS91 | |
F | LYS91 |
site_id | SWS_FT_FI14 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
M | TYR41 | |
E | TYR41 |
site_id | SWS_FT_FI15 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 |
Chain | Residue | Details |
M | LYS56 | |
M | LYS79 | |
E | LYS56 | |
E | LYS79 |
site_id | SWS_FT_FI16 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
M | SER57 | |
E | SER57 |
site_id | SWS_FT_FI17 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
E | THR80 | |
E | THR107 | |
M | THR80 | |
M | THR107 |
site_id | SWS_FT_FI18 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P84243 |
Chain | Residue | Details |
M | SER86 | |
E | SER86 |
site_id | SWS_FT_FI19 |
Number of Residues | 1 |
Details | MOD_RES: N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
M | LYS115 | |
E | LYS115 |
site_id | SWS_FT_FI20 |
Number of Residues | 1 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
M | LYS122 | |
E | LYS122 |
site_id | SWS_FT_FI21 |
Number of Residues | 1 |
Details | LIPID: S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
M | CYS110 | |
E | CYS110 |