6RYU
Nucleosome-CHD4 complex structure (two CHD4 copies)
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 |
V | 0003677 | molecular_function | DNA binding |
V | 0005524 | molecular_function | ATP binding |
V | 0006338 | biological_process | chromatin remodeling |
V | 0140658 | molecular_function | ATP-dependent chromatin remodeler activity |
W | 0003677 | molecular_function | DNA binding |
W | 0005524 | molecular_function | ATP binding |
W | 0006338 | biological_process | chromatin remodeling |
W | 0140658 | molecular_function | ATP-dependent chromatin remodeler activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 12 |
Details | binding site for residue ANP W 2201 |
Chain | Residue |
W | HIS727 |
W | ARG1162 |
W | ILE1163 |
W | MG2202 |
W | MET753 |
W | GLY754 |
W | GLY756 |
W | LYS757 |
W | THR758 |
W | VAL759 |
W | TRP797 |
W | ARG1159 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue MG W 2202 |
Chain | Residue |
W | ASP873 |
W | GLU874 |
W | ANP2201 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue ZN W 2203 |
Chain | Residue |
W | CYS452 |
W | CYS455 |
W | HIS472 |
W | CYS475 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue ZN W 2204 |
Chain | Residue |
W | CYS464 |
W | CYS467 |
W | SER469 |
W | CYS490 |
W | CYS493 |
site_id | AC5 |
Number of Residues | 12 |
Details | binding site for residue ANP V 2201 |
Chain | Residue |
V | HIS727 |
V | MET753 |
V | GLY754 |
V | GLY756 |
V | LYS757 |
V | THR758 |
V | VAL759 |
V | TRP797 |
V | ARG1159 |
V | ARG1162 |
V | ILE1163 |
V | MG2202 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue MG V 2202 |
Chain | Residue |
V | ASP873 |
V | GLU874 |
V | ANP2201 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue ZN V 2203 |
Chain | Residue |
V | CYS452 |
V | CYS455 |
V | HIS472 |
V | CYS475 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue ZN V 2204 |
Chain | Residue |
V | CYS464 |
V | CYS467 |
V | SER469 |
V | CYS490 |
V | CYS493 |
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 | PS00598 |
Number of Residues | 21 |
Details | CHROMO_1 Chromo domain signature. FfVKWqGMsywhc.SWVSelqL |
Chain | Residue | Details |
W | PHE543-LEU563 | |
W | TYR640-VAL659 |
site_id | PS00690 |
Number of Residues | 10 |
Details | DEAH_ATP_HELICASE DEAH-box subfamily ATP-dependent helicases signature. AcLIVDEAHR |
Chain | Residue | Details |
W | ALA868-ARG877 |
site_id | PS00959 |
Number of Residues | 9 |
Details | HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI |
Chain | Residue | Details |
A | PRO66-ILE74 |
site_id | PS01359 |
Number of Residues | 42 |
Details | ZF_PHD_1 Zinc finger PHD-type signature. CevCqqggei.......................................IlCdt..Cpra.YHmvCldpdmekapegk.................................WsCphC |
Chain | Residue | Details |
W | CYS373-CYS414 | |
W | CYS452-CYS493 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 94 |
Details | ZN_FING: PHD-type 1 => ECO:0000255|PROSITE-ProRule:PRU00146 |
Chain | Residue | Details |
W | GLN370-GLU417 | |
V | GLN370-GLU417 | |
D | LYS12 | |
D | LYS17 | |
H | LYS2 | |
H | LYS9 | |
H | LYS12 | |
H | LYS17 |
site_id | SWS_FT_FI2 |
Number of Residues | 94 |
Details | ZN_FING: PHD-type 2 => ECO:0000255|PROSITE-ProRule:PRU00146 |
Chain | Residue | Details |
W | MET449-PRO496 | |
V | MET449-PRO496 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00541 |
Chain | Residue | Details |
W | ASP751 | |
V | ASP751 | |
G | LYS9 | |
G | LYS95 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692 |
Chain | Residue | Details |
W | SER44 | |
V | SER44 | |
H | LYS117 |
site_id | SWS_FT_FI5 |
Number of Residues | 6 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
W | SER303 | |
W | SER1753 | |
W | SER1818 | |
V | SER303 | |
V | SER1753 | |
V | SER1818 | |
F | LYS44 | |
F | LYS79 |
site_id | SWS_FT_FI6 |
Number of Residues | 8 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692 |
Chain | Residue | Details |
W | SER308 | |
W | SER309 | |
W | SER310 | |
W | SER319 | |
V | SER308 | |
V | SER309 | |
V | SER310 | |
V | SER319 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
W | THR367 | |
V | THR367 | |
F | LYS31 | |
F | LYS91 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:21406692 |
Chain | Residue | Details |
W | SER428 | |
V | SER428 | |
C | LYS15 | |
C | LYS119 | |
G | LYS13 | |
G | LYS15 | |
G | LYS119 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
W | SER515 | |
V | SER515 | |
F | TYR51 | |
F | TYR88 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:21406692 |
Chain | Residue | Details |
W | THR517 | |
E | LYS64 | |
V | THR517 | |
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: Phosphothreonine => ECO:0007744|PubMed:18669648 |
Chain | Residue | Details |
W | THR529 | |
V | THR529 |
site_id | SWS_FT_FI12 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
W | SER531 | |
V | SER531 |
site_id | SWS_FT_FI13 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
W | THR703 | |
V | THR703 | |
F | LYS91 |
site_id | SWS_FT_FI14 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q6PDQ2 |
Chain | Residue | Details |
W | SER1425 | |
V | SER1425 |
site_id | SWS_FT_FI15 |
Number of Residues | 6 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
W | SER1524 | |
W | SER1786 | |
W | SER1792 | |
V | SER1524 | |
V | SER1786 | |
V | SER1792 |
site_id | SWS_FT_FI16 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:17525332 |
Chain | Residue | Details |
W | SER1565 | |
V | SER1565 |
site_id | SWS_FT_FI17 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q12873 |
Chain | Residue | Details |
W | SER1586 | |
V | SER1586 | |
E | THR80 | |
E | THR107 |
site_id | SWS_FT_FI18 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
W | SER1747 | |
V | SER1747 |
site_id | SWS_FT_FI19 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
W | SER1751 | |
V | SER1751 |
site_id | SWS_FT_FI20 |
Number of Residues | 4 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q6PDQ2 |
Chain | Residue | Details |
W | THR1758 | |
W | THR1765 | |
V | THR1758 | |
V | THR1765 |
site_id | SWS_FT_FI21 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
W | THR1769 | |
V | THR1769 |
site_id | SWS_FT_FI22 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
W | LYS1859 | |
V | LYS1859 |
site_id | SWS_FT_FI23 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
W | THR1869 | |
V | THR1869 |
site_id | SWS_FT_FI24 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
W | THR1895 | |
V | THR1895 |
site_id | SWS_FT_FI25 |
Number of Residues | 38 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 |
Chain | Residue | Details |
W | LYS133 | |
W | LYS1455 | |
W | LYS1744 | |
W | LYS1745 | |
W | LYS1800 | |
W | LYS1822 | |
W | LYS1833 | |
W | LYS1852 | |
W | LYS1876 | |
W | LYS1903 | |
W | LYS2081 | |
V | LYS133 | |
V | LYS146 | |
V | LYS179 | |
V | LYS297 | |
V | LYS304 | |
V | LYS696 | |
V | LYS1428 | |
V | LYS1444 | |
V | LYS1455 | |
W | LYS146 | |
V | LYS1744 | |
V | LYS1745 | |
V | LYS1800 | |
V | LYS1822 | |
V | LYS1833 | |
V | LYS1852 | |
V | LYS1876 | |
V | LYS1903 | |
V | LYS2081 | |
W | LYS179 | |
W | LYS297 | |
W | LYS304 | |
W | LYS696 | |
W | LYS1428 | |
W | LYS1444 |
site_id | SWS_FT_FI26 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0000250|UniProtKB:Q12873 |
Chain | Residue | Details |
W | LYS618 | |
V | LYS618 |
site_id | SWS_FT_FI27 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733 |
Chain | Residue | Details |
W | LYS711 | |
V | LYS711 |
site_id | SWS_FT_FI28 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25114211, ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733 |
Chain | Residue | Details |
W | LYS1520 | |
V | LYS1520 |
site_id | SWS_FT_FI29 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:28112733 |
Chain | Residue | Details |
W | LYS1781 | |
V | LYS1781 |
site_id | SWS_FT_FI30 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733 |
Chain | Residue | Details |
W | LYS1788 | |
V | LYS1788 |
site_id | SWS_FT_FI31 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733 |
Chain | Residue | Details |
W | LYS1859 | |
V | LYS1859 |
site_id | SWS_FT_FI32 |
Number of Residues | 4 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733 |
Chain | Residue | Details |
W | LYS1863 | |
W | LYS1886 | |
V | LYS1863 | |
V | LYS1886 |