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 | 0031492 | molecular_function | nucleosomal DNA binding |
| A | 0031507 | biological_process | heterochromatin formation |
| 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 | 0031507 | biological_process | heterochromatin formation |
| 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 | 0002227 | biological_process | innate immune response in mucosa |
| D | 0003677 | molecular_function | DNA binding |
| D | 0005515 | molecular_function | protein binding |
| D | 0005615 | cellular_component | extracellular space |
| D | 0005634 | cellular_component | nucleus |
| D | 0005694 | cellular_component | chromosome |
| D | 0006325 | biological_process | chromatin organization |
| D | 0019731 | biological_process | antibacterial humoral response |
| D | 0030527 | molecular_function | structural constituent of chromatin |
| D | 0031507 | biological_process | heterochromatin formation |
| D | 0046982 | molecular_function | protein heterodimerization activity |
| D | 0061844 | biological_process | antimicrobial humoral immune response mediated by antimicrobial peptide |
| 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 | 0031492 | molecular_function | nucleosomal DNA binding |
| E | 0031507 | biological_process | heterochromatin formation |
| 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 | 0031507 | biological_process | heterochromatin formation |
| 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 | 0002227 | biological_process | innate immune response in mucosa |
| H | 0003677 | molecular_function | DNA binding |
| H | 0005515 | molecular_function | protein binding |
| H | 0005615 | cellular_component | extracellular space |
| H | 0005634 | cellular_component | nucleus |
| H | 0005694 | cellular_component | chromosome |
| H | 0006325 | biological_process | chromatin organization |
| H | 0019731 | biological_process | antibacterial humoral response |
| H | 0030527 | molecular_function | structural constituent of chromatin |
| H | 0031507 | biological_process | heterochromatin formation |
| H | 0046982 | molecular_function | protein heterodimerization activity |
| H | 0061844 | biological_process | antimicrobial humoral immune response mediated by antimicrobial peptide |
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 | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q71DI3","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":"P84228","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","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-glutaryllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Lipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P68431","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| 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_FI13 |
| 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_FI14 |
| 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_FI15 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| 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_FI17 |
| 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_FI18 |
| 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_FI19 |
| 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_FI20 |
| Number of Residues | 4 |
| Details | DNA binding: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI21 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI22 |
| 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_FI23 |
| 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_FI24 |
| 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_FI25 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N5-methylglutamine","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI26 |
| 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_FI27 |
| Number of Residues | 7 |
| 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_FI28 |
| 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_FI29 |
| 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 |
