6XJD
Two mouse cGAS catalytic domain binding to human assembled nucleosome
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 | 0005576 | cellular_component | extracellular region |
A | 0005634 | cellular_component | nucleus |
A | 0005654 | cellular_component | nucleoplasm |
A | 0005694 | cellular_component | chromosome |
A | 0006325 | biological_process | chromatin organization |
A | 0006334 | biological_process | nucleosome assembly |
A | 0030527 | molecular_function | structural constituent of chromatin |
A | 0046982 | molecular_function | protein heterodimerization activity |
A | 0070062 | cellular_component | extracellular exosome |
B | 0000781 | cellular_component | chromosome, telomeric region |
B | 0000786 | cellular_component | nucleosome |
B | 0003677 | molecular_function | DNA binding |
B | 0003723 | molecular_function | RNA binding |
B | 0005515 | molecular_function | protein binding |
B | 0005576 | cellular_component | extracellular region |
B | 0005634 | cellular_component | nucleus |
B | 0005654 | cellular_component | nucleoplasm |
B | 0005694 | cellular_component | chromosome |
B | 0006325 | biological_process | chromatin organization |
B | 0006334 | biological_process | nucleosome assembly |
B | 0016020 | cellular_component | membrane |
B | 0030527 | molecular_function | structural constituent of chromatin |
B | 0032200 | biological_process | telomere organization |
B | 0032991 | cellular_component | protein-containing complex |
B | 0043505 | cellular_component | CENP-A containing nucleosome |
B | 0045653 | biological_process | negative regulation of megakaryocyte differentiation |
B | 0046982 | molecular_function | protein heterodimerization activity |
B | 0061644 | biological_process | protein localization to CENP-A containing chromatin |
B | 0070062 | cellular_component | extracellular exosome |
C | 0000786 | cellular_component | nucleosome |
C | 0003677 | molecular_function | DNA binding |
C | 0005515 | molecular_function | protein binding |
C | 0005634 | cellular_component | nucleus |
C | 0005694 | cellular_component | chromosome |
C | 0008150 | biological_process | biological_process |
C | 0019899 | molecular_function | enzyme binding |
C | 0030527 | molecular_function | structural constituent of chromatin |
C | 0031492 | molecular_function | nucleosomal DNA binding |
C | 0031507 | biological_process | heterochromatin formation |
C | 0046982 | molecular_function | protein heterodimerization activity |
C | 0070062 | cellular_component | extracellular exosome |
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 | 0005654 | cellular_component | nucleoplasm |
D | 0005694 | cellular_component | chromosome |
D | 0005829 | cellular_component | cytosol |
D | 0006334 | biological_process | nucleosome assembly |
D | 0019731 | biological_process | antibacterial humoral response |
D | 0030527 | molecular_function | structural constituent of chromatin |
D | 0042742 | biological_process | defense response to bacterium |
D | 0042802 | molecular_function | identical protein binding |
D | 0046982 | molecular_function | protein heterodimerization activity |
D | 0050830 | biological_process | defense response to Gram-positive bacterium |
D | 0061844 | biological_process | antimicrobial humoral immune response mediated by antimicrobial peptide |
D | 0070062 | cellular_component | extracellular exosome |
E | 0000786 | cellular_component | nucleosome |
E | 0003677 | molecular_function | DNA binding |
E | 0005515 | molecular_function | protein binding |
E | 0005576 | cellular_component | extracellular region |
E | 0005634 | cellular_component | nucleus |
E | 0005654 | cellular_component | nucleoplasm |
E | 0005694 | cellular_component | chromosome |
E | 0006325 | biological_process | chromatin organization |
E | 0006334 | biological_process | nucleosome assembly |
E | 0030527 | molecular_function | structural constituent of chromatin |
E | 0046982 | molecular_function | protein heterodimerization activity |
E | 0070062 | cellular_component | extracellular exosome |
F | 0000781 | cellular_component | chromosome, telomeric region |
F | 0000786 | cellular_component | nucleosome |
F | 0003677 | molecular_function | DNA binding |
F | 0003723 | molecular_function | RNA binding |
F | 0005515 | molecular_function | protein binding |
F | 0005576 | cellular_component | extracellular region |
F | 0005634 | cellular_component | nucleus |
F | 0005654 | cellular_component | nucleoplasm |
F | 0005694 | cellular_component | chromosome |
F | 0006325 | biological_process | chromatin organization |
F | 0006334 | biological_process | nucleosome assembly |
F | 0016020 | cellular_component | membrane |
F | 0030527 | molecular_function | structural constituent of chromatin |
F | 0032200 | biological_process | telomere organization |
F | 0032991 | cellular_component | protein-containing complex |
F | 0043505 | cellular_component | CENP-A containing nucleosome |
F | 0045653 | biological_process | negative regulation of megakaryocyte differentiation |
F | 0046982 | molecular_function | protein heterodimerization activity |
F | 0061644 | biological_process | protein localization to CENP-A containing chromatin |
F | 0070062 | cellular_component | extracellular exosome |
G | 0000786 | cellular_component | nucleosome |
G | 0003677 | molecular_function | DNA binding |
G | 0005515 | molecular_function | protein binding |
G | 0005634 | cellular_component | nucleus |
G | 0005694 | cellular_component | chromosome |
G | 0008150 | biological_process | biological_process |
G | 0019899 | molecular_function | enzyme binding |
G | 0030527 | molecular_function | structural constituent of chromatin |
G | 0031492 | molecular_function | nucleosomal DNA binding |
G | 0031507 | biological_process | heterochromatin formation |
G | 0046982 | molecular_function | protein heterodimerization activity |
G | 0070062 | cellular_component | extracellular exosome |
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 | 0005654 | cellular_component | nucleoplasm |
H | 0005694 | cellular_component | chromosome |
H | 0005829 | cellular_component | cytosol |
H | 0006334 | biological_process | nucleosome assembly |
H | 0019731 | biological_process | antibacterial humoral response |
H | 0030527 | molecular_function | structural constituent of chromatin |
H | 0042742 | biological_process | defense response to bacterium |
H | 0042802 | molecular_function | identical protein binding |
H | 0046982 | molecular_function | protein heterodimerization activity |
H | 0050830 | biological_process | defense response to Gram-positive bacterium |
H | 0061844 | biological_process | antimicrobial humoral immune response mediated by antimicrobial peptide |
H | 0070062 | cellular_component | extracellular exosome |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | binding site for residue ZN K 601 |
Chain | Residue |
K | CYS385 |
K | LYS391 |
K | LYS395 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue ZN L 601 |
Chain | Residue |
L | CYS385 |
L | LYS391 |
L | LYS395 |
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 | ARG92-GLY114 |
site_id | PS00959 |
Number of Residues | 9 |
Details | HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI |
Chain | Residue | Details |
A | PRO66-ILE74 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:23647843 |
Chain | Residue | Details |
K | THR197 | |
L | SER199 | |
L | GLU211 | |
L | ASP213 | |
L | ASP307 | |
L | GLU371 | |
L | LYS402 | |
L | SER420 | |
K | SER199 | |
K | GLU211 | |
K | ASP213 | |
K | ASP307 | |
K | GLU371 | |
K | LYS402 | |
K | SER420 | |
L | THR197 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:24332030, ECO:0007744|PDB:4LEZ |
Chain | Residue | Details |
K | GLY290 | |
H | LYS11 | |
H | LYS15 | |
H | LYS16 | |
H | LYS20 | |
H | LYS23 | |
H | LYS43 | |
H | LYS85 | |
K | LYS350 | |
K | ARG364 | |
L | GLY290 | |
L | LYS350 | |
L | ARG364 | |
D | LYS43 | |
D | LYS85 | |
H | LYS5 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:23647843, ECO:0000269|PubMed:24332030, ECO:0000269|PubMed:24462292, ECO:0000269|PubMed:28902841, ECO:0000269|PubMed:28963528, ECO:0000269|PubMed:32814054, ECO:0000269|PubMed:32911481, ECO:0000269|PubMed:32913000, ECO:0007744|PDB:5N6I, ECO:0007744|PDB:5XZB, ECO:0007744|PDB:5XZE, ECO:0007744|PDB:5XZG, ECO:0007744|PDB:6X59, ECO:0007744|PDB:7BUJ, ECO:0007744|PDB:7BUM, ECO:0007744|PDB:7BUQ, ECO:0007744|PDB:7JO9, ECO:0007744|PDB:7JOA |
Chain | Residue | Details |
K | HIS378 | |
K | CYS384 | |
L | HIS378 | |
L | CYS384 | |
G | LYS74 | |
G | LYS75 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:23647843, ECO:0000269|PubMed:24332030, ECO:0000269|PubMed:24462292, ECO:0000269|PubMed:28902841, ECO:0000269|PubMed:28963528, ECO:0000269|PubMed:32814054, ECO:0000269|PubMed:32911481, ECO:0000269|PubMed:32913000, ECO:0007744|PDB:5N6I, ECO:0007744|PDB:5XZB, ECO:0007744|PDB:5XZE, ECO:0007744|PDB:5XZG, ECO:0007744|PDB:6XJD, ECO:0007744|PDB:7BUJ, ECO:0007744|PDB:7BUM, ECO:0007744|PDB:7BUQ, ECO:0007744|PDB:7JO9, ECO:0007744|PDB:7JOA |
Chain | Residue | Details |
K | CYS385 | |
L | CYS385 | |
G | LYS9 | |
G | LYS95 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:23647843, ECO:0000269|PubMed:24332030, ECO:0000269|PubMed:24462292, ECO:0000269|PubMed:28902841, ECO:0000269|PubMed:28963528, ECO:0000269|PubMed:32814054, ECO:0000269|PubMed:32911480, ECO:0000269|PubMed:32911481, ECO:0000269|PubMed:32913000, ECO:0007744|PDB:5N6I, ECO:0007744|PDB:5XZB, ECO:0007744|PDB:5XZE, ECO:0007744|PDB:5XZG, ECO:0007744|PDB:6X5A, ECO:0007744|PDB:7BUJ, ECO:0007744|PDB:7BUM, ECO:0007744|PDB:7BUQ, ECO:0007744|PDB:7JO9, ECO:0007744|PDB:7JOA |
Chain | Residue | Details |
K | CYS392 | |
L | CYS392 | |
B | LYS44 | |
F | LYS8 | |
F | LYS16 | |
F | LYS44 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | SITE: Arginine-anchor => ECO:0000269|PubMed:31808743, ECO:0000269|PubMed:32911480, ECO:0000269|PubMed:32911481, ECO:0000269|PubMed:32913000 |
Chain | Residue | Details |
K | ARG241 | |
L | ARG241 | |
B | LYS77 | |
B | LYS91 | |
F | LYS12 | |
F | LYS31 | |
F | LYS77 | |
F | LYS91 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | SITE: Cleavage; by CASP3 => ECO:0000250|UniProtKB:Q8N884 |
Chain | Residue | Details |
K | ASP307 | |
L | ASP307 | |
D | LYS120 | |
H | LYS34 | |
H | LYS116 | |
H | LYS120 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: PolyADP-ribosyl glutamic acid => ECO:0000269|PubMed:35460603 |
Chain | Residue | Details |
K | GLU176 | |
L | GLU176 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q8N884 |
Chain | Residue | Details |
K | SER199 | |
L | SER199 | |
C | LYS125 | |
G | LYS118 | |
G | LYS119 | |
G | LYS125 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q8N884 |
Chain | Residue | Details |
K | TYR201 | |
L | TYR201 | |
H | LYS46 | |
H | LYS108 |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | MOD_RES: 5-glutamyl polyglutamate => ECO:0000269|PubMed:26829768 |
Chain | Residue | Details |
K | GLU272 | |
L | GLU272 |
site_id | SWS_FT_FI12 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine; by CDK1 and PKB => ECO:0000269|PubMed:26440888, ECO:0000269|PubMed:32351706 |
Chain | Residue | Details |
K | SER291 | |
L | SER291 | |
G | LYS119 |
site_id | SWS_FT_FI13 |
Number of Residues | 2 |
Details | MOD_RES: 5-glutamyl glutamate => ECO:0000269|PubMed:26829768 |
Chain | Residue | Details |
K | GLU302 | |
L | GLU302 | |
H | ARG86 | |
H | ARG92 |
site_id | SWS_FT_FI14 |
Number of Residues | 6 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q8N884 |
Chain | Residue | Details |
K | LYS372 | |
K | LYS382 | |
K | LYS402 | |
L | LYS372 | |
L | LYS382 | |
L | LYS402 |
site_id | SWS_FT_FI15 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:32474700 |
Chain | Residue | Details |
K | SER420 | |
L | SER420 | |
F | LYS91 |
site_id | SWS_FT_FI16 |
Number of Residues | 2 |
Details | MOD_RES: N6-methyllysine => ECO:0000269|PubMed:35210392 |
Chain | Residue | Details |
K | LYS491 | |
L | LYS491 | |
B | LYS79 | |
F | LYS20 | |
F | LYS59 | |
F | LYS79 |
site_id | SWS_FT_FI17 |
Number of Residues | 6 |
Details | LIPID: S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q8N884 |
Chain | Residue | Details |
K | CYS392 | |
K | CYS393 | |
K | CYS459 | |
L | CYS392 | |
L | CYS393 | |
L | CYS459 |
site_id | SWS_FT_FI18 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269|PubMed:27637147 |
Chain | Residue | Details |
K | LYS217 | |
L | LYS217 |
site_id | SWS_FT_FI19 |
Number of Residues | 4 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:27637147, ECO:0000269|PubMed:32457395 |
Chain | Residue | Details |
D | LYS34 | |
K | LYS464 | |
L | LYS464 |
site_id | SWS_FT_FI20 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:27637147, ECO:0000269|PubMed:32457395 |
Chain | Residue | Details |
K | LYS271 | |
L | LYS271 |
site_id | SWS_FT_FI21 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:29426904 |
Chain | Residue | Details |
K | LYS335 | |
L | LYS335 |
site_id | SWS_FT_FI22 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:Q8N884 |
Chain | Residue | Details |
K | LYS372 | |
L | LYS372 |
site_id | SWS_FT_FI23 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269|PubMed:28095500 |
Chain | Residue | Details |
K | LYS382 | |
L | LYS382 |
site_id | SWS_FT_FI24 |
Number of Residues | 4 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:Q8N884 |
Chain | Residue | Details |
K | LYS399 | |
K | LYS402 | |
L | LYS399 | |
L | LYS402 |
site_id | SWS_FT_FI25 |
Number of Residues | 4 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:38418882 |
Chain | Residue | Details |
K | LYS409 | |
K | LYS410 | |
L | LYS409 | |
L | LYS410 |
site_id | SWS_FT_FI26 |
Number of Residues | 2 |
Details | LIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:21076176 |
Chain | Residue | Details |
A | ALA110 | |
E | ALA110 |