1S32
Molecular Recognition of the Nucleosomal 'Supergroove'
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 2001 |
Chain | Residue |
D | VAL1245 |
E | ASP677 |
E | HOH3391 |
E | HOH3393 |
E | HOH3394 |
F | HOH3392 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN J 2002 |
Chain | Residue |
J | HOH3397 |
J | HOH3398 |
J | HOH3399 |
I | HOH3396 |
J | DG246 |
J | HOH3395 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MN I 2003 |
Chain | Residue |
I | DG70 |
I | DG71 |
I | HOH3400 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MN I 2004 |
Chain | Residue |
I | DG134 |
I | HOH3401 |
I | HOH3402 |
I | HOH3403 |
site_id | AC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE MN J 2005 |
Chain | Residue |
J | DG280 |
J | HOH3641 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MN I 2006 |
Chain | Residue |
I | DG100 |
I | HOH3526 |
I | HOH3832 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MN I 2007 |
Chain | Residue |
I | DG39 |
I | DG40 |
I | HOH3153 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MN J 2008 |
Chain | Residue |
J | DT266 |
J | DG267 |
J | HOH3047 |
J | HOH3411 |
site_id | AC9 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE MN I 2009 |
Chain | Residue |
I | DG121 |
site_id | BC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE MN J 2010 |
Chain | Residue |
J | DG217 |
J | HOH3491 |
site_id | BC2 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE MN J 2011 |
Chain | Residue |
J | DG227 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MN I 2012 |
Chain | Residue |
I | HOH3821 |
J | HOH3295 |
J | HOH3820 |
J | HOH3833 |
site_id | BC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MN J 2013 |
Chain | Residue |
J | DG185 |
J | DG186 |
J | HOH3499 |
site_id | BC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MN I 2014 |
Chain | Residue |
I | DG137 |
I | DG138 |
I | HOH3233 |
site_id | BC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL E 2015 |
Chain | Residue |
E | PRO721 |
E | LYS722 |
site_id | BC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CL G 2016 |
Chain | Residue |
G | GLY1044 |
G | ALA1045 |
G | GLY1046 |
G | ALA1047 |
H | THR1487 |
H | SER1488 |
site_id | BC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL A 2017 |
Chain | Residue |
A | PRO521 |
A | LYS522 |
site_id | BC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL D 2018 |
Chain | Residue |
C | GLY846 |
C | ALA847 |
D | THR1287 |
D | SER1288 |
site_id | CC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE IMT I 1601 |
Chain | Residue |
I | DG31 |
I | DT32 |
I | PYB1602 |
I | PYB1608 |
I | PYB1609 |
site_id | CC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PYB I 1602 |
Chain | Residue |
I | DT32 |
I | DG33 |
I | IMT1601 |
I | IMT1603 |
I | PYB1607 |
I | PYB1608 |
site_id | CC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE IMT I 1603 |
Chain | Residue |
I | DG33 |
I | DT34 |
I | DA35 |
I | PYB1602 |
I | PYB1604 |
site_id | CC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PYB I 1604 |
Chain | Residue |
I | DT34 |
I | DA35 |
I | DT36 |
I | IMT1603 |
I | ABU1605 |
I | PYB1606 |
I | HOH3243 |
site_id | CC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ABU I 1605 |
Chain | Residue |
I | PYB1604 |
I | PYB1606 |
J | DA259 |
J | DC260 |
J | OGG1700 |
site_id | CC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PYB I 1606 |
Chain | Residue |
I | PYB1604 |
I | ABU1605 |
I | PYB1607 |
J | DA259 |
J | DC260 |
J | DA261 |
J | OGG1700 |
site_id | CC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PYB I 1607 |
Chain | Residue |
I | PYB1602 |
I | PYB1606 |
I | PYB1608 |
J | DC260 |
J | DA261 |
site_id | CC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PYB I 1608 |
Chain | Residue |
I | IMT1601 |
I | PYB1602 |
I | PYB1607 |
I | PYB1609 |
J | DA261 |
J | DC262 |
J | DT263 |
site_id | CC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PYB I 1609 |
Chain | Residue |
I | DG31 |
I | IMT1601 |
I | PYB1608 |
I | BAL1610 |
J | DC262 |
J | DT263 |
site_id | DC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE BAL I 1610 |
Chain | Residue |
I | DA30 |
I | DG31 |
I | PYB1609 |
I | DIB1611 |
J | DT263 |
site_id | DC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE DIB I 1611 |
Chain | Residue |
I | DA29 |
I | DA30 |
I | BAL1610 |
J | DT265 |
J | DT266 |
site_id | DC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE IMT I 1621 |
Chain | Residue |
I | PYB1622 |
I | PYB1628 |
I | PYB1629 |
J | DT178 |
site_id | DC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PYB I 1622 |
Chain | Residue |
I | IMT1621 |
I | IMT1623 |
I | PYB1627 |
I | PYB1628 |
J | DT178 |
J | DG179 |
site_id | DC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE IMT I 1623 |
Chain | Residue |
I | PYB1622 |
I | PYB1624 |
I | PYB1627 |
J | DG179 |
J | DT180 |
J | DA181 |
site_id | DC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PYB I 1624 |
Chain | Residue |
I | DA113 |
I | IMT1623 |
I | ABU1625 |
I | PYB1626 |
J | DT180 |
J | DA181 |
J | DT182 |
site_id | DC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ABU I 1625 |
Chain | Residue |
I | DA113 |
I | PYB1624 |
I | PYB1626 |
J | DA181 |
J | OGG1700 |
site_id | DC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PYB I 1626 |
Chain | Residue |
I | DA113 |
I | DC114 |
I | DA115 |
I | PYB1624 |
I | ABU1625 |
I | PYB1627 |
J | OGG1700 |
site_id | DC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PYB I 1627 |
Chain | Residue |
I | DC114 |
I | DA115 |
I | DC116 |
I | PYB1622 |
I | IMT1623 |
I | PYB1626 |
I | PYB1628 |
site_id | EC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PYB I 1628 |
Chain | Residue |
I | DA115 |
I | DC116 |
I | DT117 |
I | IMT1621 |
I | PYB1622 |
I | PYB1627 |
I | PYB1629 |
site_id | EC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PYB I 1629 |
Chain | Residue |
G | LYS1013 |
I | DC116 |
I | DT117 |
I | DT118 |
I | IMT1621 |
I | PYB1628 |
I | BAL1630 |
J | DG177 |
site_id | EC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE BAL I 1630 |
Chain | Residue |
G | ALA1014 |
I | PYB1629 |
I | DIB1631 |
J | DA176 |
J | DG177 |
site_id | EC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE DIB I 1631 |
Chain | Residue |
I | DT119 |
I | DT120 |
I | BAL1630 |
J | DA175 |
J | DA176 |
site_id | EC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE OGG J 1700 |
Chain | Residue |
I | DA113 |
I | ABU1605 |
I | PYB1606 |
I | ABU1625 |
I | PYB1626 |
J | DA259 |
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 | 8 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P0C1H4 |
Chain | Residue | Details |
D | LYS1202 | |
D | LYS1209 | |
D | LYS1212 | |
D | LYS1217 | |
H | LYS1402 | |
H | LYS1409 | |
H | LYS1412 | |
H | LYS1417 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:12757711 |
Chain | Residue | Details |
D | SER1211 | |
H | SER1411 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | CARBOHYD: O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 |
Chain | Residue | Details |
D | SER1309 | |
H | SER1509 | |
G | LYS1009 | |
G | LYS1095 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0C1H4 |
Chain | Residue | Details |
D | LYS1317 | |
G | LYS1036 | |
H | LYS1517 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 |
Chain | Residue | Details |
C | LYS874 | |
C | LYS875 | |
G | LYS1074 | |
G | LYS1075 | |
F | LYS208 | |
F | LYS216 | |
F | LYS244 | |
F | LYS279 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: N5-methylglutamine => ECO:0000250 |
Chain | Residue | Details |
C | GLN904 | |
G | GLN1104 | |
F | LYS212 | |
F | LYS220 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8 |
Chain | Residue | Details |
C | LYS918 | |
G | LYS1118 | |
F | LYS231 | |
F | LYS291 |
site_id | SWS_FT_FI8 |
Number of Residues | 8 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250 |
Chain | Residue | Details |
C | LYS813 | |
F | SER247 | |
C | LYS815 | |
C | LYS919 | |
G | LYS1013 | |
G | LYS1015 | |
G | LYS1119 |
site_id | SWS_FT_FI9 |
Number of Residues | 4 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P62805 |
Chain | Residue | Details |
B | TYR51 | |
B | TYR88 | |
F | TYR251 | |
F | TYR288 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | MOD_RES: N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 |
Chain | Residue | Details |
B | LYS59 | |
E | LYS664 | |
F | LYS259 | |
A | LYS427 | |
A | LYS436 | |
A | LYS464 | |
E | LYS618 | |
E | LYS623 | |
E | LYS627 | |
E | LYS636 |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P62805 |
Chain | Residue | Details |
B | LYS77 | |
F | LYS277 |
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 | LYS231 |
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 | LYS437 | |
B | LYS91 | |
F | LYS291 |
site_id | SWS_FT_FI14 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | TYR441 | |
E | TYR641 |
site_id | SWS_FT_FI15 |
Number of Residues | 4 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 |
Chain | Residue | Details |
A | LYS456 | |
A | LYS479 | |
E | LYS656 | |
E | LYS679 |
site_id | SWS_FT_FI16 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | SER457 | |
E | SER657 |
site_id | SWS_FT_FI17 |
Number of Residues | 4 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | THR480 | |
A | THR507 | |
E | THR680 | |
E | THR707 |
site_id | SWS_FT_FI18 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P84243 |
Chain | Residue | Details |
A | SER486 | |
E | SER686 |
site_id | SWS_FT_FI19 |
Number of Residues | 2 |
Details | MOD_RES: N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | LYS515 | |
E | LYS715 |
site_id | SWS_FT_FI20 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | LYS522 | |
E | LYS722 |
site_id | SWS_FT_FI21 |
Number of Residues | 2 |
Details | LIPID: S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | CYS510 | |
E | CYS710 |