8V4Y
Cryo-EM structure of singly-bound SNF2h-nucleosome complex with SNF2h at inactive SHL2 (conformation 1)
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 |
| 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 |
| C | 0000786 | cellular_component | nucleosome |
| C | 0003677 | molecular_function | DNA binding |
| C | 0005634 | cellular_component | nucleus |
| C | 0005694 | cellular_component | chromosome |
| 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 |
| 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 |
| 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 |
| G | 0000786 | cellular_component | nucleosome |
| G | 0003677 | molecular_function | DNA binding |
| G | 0005634 | cellular_component | nucleus |
| G | 0005694 | cellular_component | chromosome |
| 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 |
| W | 0000183 | biological_process | rDNA heterochromatin formation |
| W | 0000793 | cellular_component | condensed chromosome |
| W | 0001650 | cellular_component | fibrillar center |
| W | 0003677 | molecular_function | DNA binding |
| W | 0004386 | molecular_function | helicase activity |
| W | 0005515 | molecular_function | protein binding |
| W | 0005524 | molecular_function | ATP binding |
| W | 0005634 | cellular_component | nucleus |
| W | 0005654 | cellular_component | nucleoplasm |
| W | 0005677 | cellular_component | chromatin silencing complex |
| W | 0005694 | cellular_component | chromosome |
| W | 0005721 | cellular_component | pericentric heterochromatin |
| W | 0005730 | cellular_component | nucleolus |
| W | 0006275 | biological_process | regulation of DNA replication |
| W | 0006281 | biological_process | DNA repair |
| W | 0006325 | biological_process | chromatin organization |
| W | 0006334 | biological_process | nucleosome assembly |
| W | 0006338 | biological_process | chromatin remodeling |
| W | 0006346 | biological_process | DNA methylation-dependent heterochromatin formation |
| W | 0006352 | biological_process | DNA-templated transcription initiation |
| W | 0006355 | biological_process | regulation of DNA-templated transcription |
| W | 0006357 | biological_process | regulation of transcription by RNA polymerase II |
| W | 0006974 | biological_process | DNA damage response |
| W | 0008094 | molecular_function | ATP-dependent activity, acting on DNA |
| W | 0008623 | cellular_component | CHRAC |
| W | 0016479 | biological_process | negative regulation of transcription by RNA polymerase I |
| W | 0016589 | cellular_component | NURF complex |
| W | 0016590 | cellular_component | ACF complex |
| W | 0016787 | molecular_function | hydrolase activity |
| W | 0016887 | molecular_function | ATP hydrolysis activity |
| W | 0031010 | cellular_component | ISWI-type complex |
| W | 0031213 | cellular_component | RSF complex |
| W | 0031507 | biological_process | heterochromatin formation |
| W | 0035861 | cellular_component | site of double-strand break |
| W | 0042393 | molecular_function | histone binding |
| W | 0043596 | cellular_component | nuclear replication fork |
| W | 0044030 | biological_process | obsolete regulation of DNA methylation |
| W | 0045740 | biological_process | positive regulation of DNA replication |
| W | 0045893 | biological_process | positive regulation of DNA-templated transcription |
| W | 0045943 | biological_process | positive regulation of transcription by RNA polymerase I |
| W | 0045944 | biological_process | positive regulation of transcription by RNA polymerase II |
| W | 0045945 | biological_process | positive regulation of transcription by RNA polymerase III |
| W | 0090535 | cellular_component | WICH complex |
| W | 0090536 | cellular_component | NoRC complex |
| W | 0110016 | cellular_component | B-WICH complex |
| W | 0140374 | biological_process | antiviral innate immune response |
| W | 0140658 | molecular_function | ATP-dependent chromatin remodeler activity |
| W | 0140751 | molecular_function | histone octamer slider activity |
| W | 1905213 | biological_process | negative regulation of mitotic chromosome condensation |
| W | 1990830 | biological_process | cellular response to leukemia inhibitory factor |
Functional Information from PROSITE/UniProt
| 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 | PS00046 |
| Number of Residues | 7 |
| Details | HISTONE_H2A Histone H2A signature. AGLqFPV |
| Chain | Residue | Details |
| C | ALA21-VAL27 |
| 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 | 1 |
| Details | BINDING: BINDING => ECO:0000305 |
| Chain | Residue | Details |
| E | ARG17 | |
| W | ASP205 | |
| H | LYS2 | |
| H | LYS9 | |
| H | LYS12 | |
| H | LYS17 | |
| E | ARG2 | |
| F | LYS16-LYS20 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | MOD_RES: N-acetylserine => ECO:0007744|PubMed:19413330 |
| Chain | Residue | Details |
| W | SER2 | |
| F | SER1 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:17693683, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| W | SER66 | |
| G | LYS9 | |
| G | LYS95 | |
| F | ARG3 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:20068231 |
| Chain | Residue | Details |
| W | THR113 | |
| H | LYS117 | |
| F | LYS5 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| W | SER116 | |
| F | LYS8 | |
| F | LYS16 | |
| F | LYS44 | |
| F | LYS79 | |
| B | LYS16 | |
| B | LYS44 | |
| B | LYS79 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| W | SER137 | |
| F | LYS12 | |
| F | LYS20 | |
| B | LYS20 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| W | SER171 | |
| W | SER755 | |
| F | LYS31 | |
| F | LYS91 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| W | LYS440 | |
| C | LYS15 | |
| C | LYS119 | |
| G | LYS13 | |
| G | LYS15 | |
| G | LYS119 | |
| F | SER47 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692 |
| Chain | Residue | Details |
| W | SER825 | |
| B | TYR88 | |
| F | TYR51 | |
| F | TYR88 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 8 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 |
| Chain | Residue | Details |
| W | LYS83 | |
| F | LYS59 | |
| W | LYS644 | |
| W | LYS647 | |
| W | LYS694 | |
| W | LYS722 | |
| W | LYS735 | |
| W | LYS966 | |
| E | LYS36 | |
| E | LYS64 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P62805 |
| Chain | Residue | Details |
| B | LYS77 | |
| F | LYS77 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate => ECO:0000250|UniProtKB:P62805 |
| Chain | Residue | Details |
| B | LYS31 | |
| F | LYS31 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 4 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62805 |
| Chain | Residue | Details |
| A | LYS37 | |
| B | LYS91 | |
| F | LYS91 |
| 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 | ALA110 | |
| E | ALA110 |
