1M1A
LIGAND BINDING ALTERS THE STRUCTURE AND DYNAMICS OF NUCLEOSOMAL DNA
Functional Information from GO Data
| Chain | GOid | namespace | contents | 
| A | 0000786 | cellular_component | nucleosome | 
| A | 0003677 | molecular_function | DNA binding | 
| A | 0005634 | cellular_component | nucleus | 
| 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 | 0031507 | biological_process | heterochromatin formation | 
| 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 | 0005634 | cellular_component | nucleus | 
| 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 | 0031507 | biological_process | heterochromatin formation | 
| 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 301 | 
| Chain | Residue | 
| D | VAL1245 | 
| E | HOH55 | 
| E | HOH181 | 
| E | HOH182 | 
| E | ASP677 | 
| F | HOH99 | 
| site_id | AC2 | 
| Number of Residues | 2 | 
| Details | BINDING SITE FOR RESIDUE MN J 302 | 
| Chain | Residue | 
| J | DG280 | 
| J | DG281 | 
| site_id | AC3 | 
| Number of Residues | 1 | 
| Details | BINDING SITE FOR RESIDUE MN I 303 | 
| Chain | Residue | 
| I | DG134 | 
| site_id | AC4 | 
| Number of Residues | 1 | 
| Details | BINDING SITE FOR RESIDUE MN J 304 | 
| Chain | Residue | 
| J | DG216 | 
| site_id | AC5 | 
| Number of Residues | 1 | 
| Details | BINDING SITE FOR RESIDUE MN I 305 | 
| Chain | Residue | 
| I | DG71 | 
| site_id | AC6 | 
| Number of Residues | 1 | 
| Details | BINDING SITE FOR RESIDUE MN J 306 | 
| Chain | Residue | 
| J | DG267 | 
| site_id | AC7 | 
| Number of Residues | 2 | 
| Details | BINDING SITE FOR RESIDUE MN J 308 | 
| Chain | Residue | 
| J | DA245 | 
| J | DG246 | 
| site_id | AC8 | 
| Number of Residues | 1 | 
| Details | BINDING SITE FOR RESIDUE MN I 309 | 
| Chain | Residue | 
| I | DG121 | 
| site_id | AC9 | 
| Number of Residues | 2 | 
| Details | BINDING SITE FOR RESIDUE MN I 310 | 
| Chain | Residue | 
| I | DG39 | 
| I | DG40 | 
| site_id | BC1 | 
| Number of Residues | 6 | 
| Details | BINDING SITE FOR RESIDUE IMT J 1901 | 
| Chain | Residue | 
| J | DG283 | 
| J | DG284 | 
| J | DA285 | 
| J | IMT1902 | 
| J | PYB1909 | 
| J | BAL1910 | 
| site_id | BC2 | 
| Number of Residues | 7 | 
| Details | BINDING SITE FOR RESIDUE IMT J 1902 | 
| Chain | Residue | 
| J | DG284 | 
| J | DA285 | 
| J | DT286 | 
| J | IMT1901 | 
| J | PYB1903 | 
| J | PYB1908 | 
| J | PYB1909 | 
| site_id | BC3 | 
| Number of Residues | 6 | 
| Details | BINDING SITE FOR RESIDUE PYB J 1903 | 
| Chain | Residue | 
| J | DA285 | 
| J | DT286 | 
| J | IMT1902 | 
| J | PYB1904 | 
| J | PYB1907 | 
| J | PYB1908 | 
| site_id | BC4 | 
| Number of Residues | 7 | 
| Details | BINDING SITE FOR RESIDUE PYB J 1904 | 
| Chain | Residue | 
| J | DT286 | 
| J | DA287 | 
| J | DT288 | 
| J | PYB1903 | 
| J | ABU1905 | 
| J | PYB1906 | 
| J | PYB1907 | 
| site_id | BC5 | 
| Number of Residues | 5 | 
| Details | BINDING SITE FOR RESIDUE ABU J 1905 | 
| Chain | Residue | 
| I | DA7 | 
| J | DA287 | 
| J | DT288 | 
| J | PYB1904 | 
| J | PYB1906 | 
| site_id | BC6 | 
| Number of Residues | 6 | 
| Details | BINDING SITE FOR RESIDUE PYB J 1906 | 
| Chain | Residue | 
| I | DA7 | 
| I | DT8 | 
| I | DC9 | 
| J | PYB1904 | 
| J | ABU1905 | 
| J | PYB1907 | 
| site_id | BC7 | 
| Number of Residues | 7 | 
| Details | BINDING SITE FOR RESIDUE PYB J 1907 | 
| Chain | Residue | 
| I | DT8 | 
| I | DC9 | 
| I | DC10 | 
| J | PYB1903 | 
| J | PYB1904 | 
| J | PYB1906 | 
| J | PYB1908 | 
| site_id | BC8 | 
| Number of Residues | 8 | 
| Details | BINDING SITE FOR RESIDUE PYB J 1908 | 
| Chain | Residue | 
| I | DC9 | 
| I | DC10 | 
| I | DA11 | 
| J | DG284 | 
| J | IMT1902 | 
| J | PYB1903 | 
| J | PYB1907 | 
| J | PYB1909 | 
| site_id | BC9 | 
| Number of Residues | 8 | 
| Details | BINDING SITE FOR RESIDUE PYB J 1909 | 
| Chain | Residue | 
| I | DC10 | 
| I | DA11 | 
| I | DC12 | 
| J | DG283 | 
| J | IMT1901 | 
| J | IMT1902 | 
| J | PYB1908 | 
| J | BAL1910 | 
| site_id | CC1 | 
| Number of Residues | 6 | 
| Details | BINDING SITE FOR RESIDUE BAL J 1910 | 
| Chain | Residue | 
| I | DA11 | 
| J | DT282 | 
| J | DG283 | 
| J | IMT1901 | 
| J | PYB1909 | 
| J | DIB1911 | 
| site_id | CC2 | 
| Number of Residues | 2 | 
| Details | BINDING SITE FOR RESIDUE DIB J 1911 | 
| Chain | Residue | 
| J | DT282 | 
| J | BAL1910 | 
Functional Information from PROSITE/UniProt
| site_id | PS00046 | 
| Number of Residues | 7 | 
| Details | HISTONE_H2A Histone H2A signature. AGLqFPV | 
| Chain | Residue | Details | 
| C | ALA821-VAL827 | 
| 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 | LYS414-LEU420 | 
| site_id | PS00357 | 
| Number of Residues | 23 | 
| Details | HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG | 
| Chain | Residue | Details | 
| D | ARG1289-GLY1311 | 
| site_id | PS00959 | 
| Number of Residues | 9 | 
| Details | HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI | 
| Chain | Residue | Details | 
| A | PRO466-ILE474 | 
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 | 
| Number of Residues | 2 | 
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P84243","evidenceCode":"ECO:0000250"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI2 | 
| Number of Residues | 4 | 
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P84244","evidenceCode":"ECO:0000250"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI3 | 
| Number of Residues | 2 | 
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P84243","evidenceCode":"ECO:0000250"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI4 | 
| Number of Residues | 2 | 
| Details | Modified residue: {"description":"N6-methylated lysine","evidences":[{"source":"UniProtKB","id":"P84243","evidenceCode":"ECO:0000250"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI5 | 
| Number of Residues | 2 | 
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P84243","evidenceCode":"ECO:0000250"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI6 | 
| Number of Residues | 2 | 
| Details | Modified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"UniProtKB","id":"P84243","evidenceCode":"ECO:0000250"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI7 | 
| Number of Residues | 2 | 
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P84243","evidenceCode":"ECO:0000250"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI9 | 
| Number of Residues | 4 | 
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI10 | 
| Number of Residues | 5 | 
| Details | Modified residue: {"description":"N6-propionyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI11 | 
| Number of Residues | 2 | 
| Details | Modified residue: {"description":"Phosphoserine; by PAK2","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI12 | 
| Number of Residues | 4 | 
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI13 | 
| Number of Residues | 2 | 
| Details | Modified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI14 | 
| Number of Residues | 2 | 
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI15 | 
| Number of Residues | 2 | 
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI16 | 
| Number of Residues | 4 | 
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI17 | 
| Number of Residues | 4 | 
| Details | DNA binding: {} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI18 | 
| Number of Residues | 2 | 
| Details | Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI19 | 
| Number of Residues | 2 | 
| Details | Modified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine; alternate","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI20 | 
| Number of Residues | 4 | 
| Details | Modified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI21 | 
| Number of Residues | 2 | 
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI22 | 
| Number of Residues | 2 | 
| Details | Modified residue: {"description":"N5-methylglutamine","evidences":[{"evidenceCode":"ECO:0000250"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI23 | 
| Number of Residues | 2 | 
| Details | Modified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI24 | 
| Number of Residues | 5 | 
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"evidenceCode":"ECO:0000250"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI25 | 
| Number of Residues | 2 | 
| Details | Glycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"source":"UniProtKB","id":"P62807","evidenceCode":"ECO:0000250"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI26 | 
| Number of Residues | 4 | 
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P0C1H4","evidenceCode":"ECO:0000250"}]} | 
| Chain | Residue | Details | 











