7CCQ
Structure of the 1:1 cGAS-nucleosome complex
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000786 | cellular_component | nucleosome |
A | 0003677 | molecular_function | DNA binding |
A | 0030527 | molecular_function | structural constituent of chromatin |
A | 0046982 | molecular_function | protein heterodimerization activity |
B | 0003677 | molecular_function | DNA binding |
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 | 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 | 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 | 0030527 | molecular_function | structural constituent of chromatin |
E | 0046982 | molecular_function | protein heterodimerization activity |
F | 0003677 | molecular_function | DNA binding |
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 | 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 | 0030527 | molecular_function | structural constituent of chromatin |
H | 0046982 | molecular_function | protein heterodimerization activity |
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 | 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 | 6 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 |
Chain | Residue | Details |
B | LYS31 | |
B | LYS77 | |
B | LYS91 | |
F | LYS31 | |
F | LYS77 | |
F | LYS91 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: N6-propionyllysine; alternate => ECO:0000269|PubMed:17267393 |
Chain | Residue | Details |
B | LYS44 | |
F | LYS44 | |
K | LYS414 | |
G | LYS75 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine; by PAK2 => ECO:0000269|PubMed:21724829, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
B | SER47 | |
F | SER47 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455, ECO:0007744|PubMed:20068231 |
Chain | Residue | Details |
B | TYR51 | |
F | TYR51 | |
H | LYS43 | |
H | LYS85 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: N6-glutaryllysine; alternate => ECO:0000269|PubMed:31542297 |
Chain | Residue | Details |
B | LYS59 | |
F | LYS59 | |
H | LYS46 | |
H | LYS108 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62806 |
Chain | Residue | Details |
B | LYS79 | |
F | LYS79 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P62806 |
Chain | Residue | Details |
B | THR80 | |
F | THR80 | |
K | CYS404 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
B | TYR88 | |
F | TYR88 | |
H | ARG86 | |
H | ARG92 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate => ECO:0000269|PubMed:30886146 |
Chain | Residue | Details |
B | LYS31 | |
F | LYS31 |
site_id | SWS_FT_FI10 |
Number of Residues | 4 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:19818714 |
Chain | Residue | Details |
K | LYS187 | |
B | LYS91 | |
F | LYS91 |
site_id | SWS_FT_FI11 |
Number of Residues | 4 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733 |
Chain | Residue | Details |
B | LYS59 | |
B | LYS79 | |
F | LYS59 | |
F | LYS79 |
site_id | SWS_FT_FI12 |
Number of Residues | 1 |
Details | SITE: Cleavage; by CASP3 => ECO:0000269|PubMed:30878284 |
Chain | Residue | Details |
K | ASP319 | |
D | LYS120 | |
H | LYS120 |
site_id | SWS_FT_FI13 |
Number of Residues | 1 |
Details | MOD_RES: PolyADP-ribosyl aspartic acid => ECO:0000269|PubMed:35460603 |
Chain | Residue | Details |
K | ASP191 |
site_id | SWS_FT_FI14 |
Number of Residues | 2 |
Details | MOD_RES: (Microbial infection) Deamidated asparagine; by herpes simplex virus 1/HHV-1 UL37 => ECO:0000269|PubMed:30092200 |
Chain | Residue | Details |
K | ASN210 | |
K | ASN389 |
site_id | SWS_FT_FI15 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:33273464 |
Chain | Residue | Details |
K | SER213 |
site_id | SWS_FT_FI16 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine; by BLK => ECO:0000269|PubMed:30356214 |
Chain | Residue | Details |
K | TYR215 |
site_id | SWS_FT_FI17 |
Number of Residues | 1 |
Details | MOD_RES: 5-glutamyl polyglutamate => ECO:0000250|UniProtKB:Q8C6L5 |
Chain | Residue | Details |
K | GLU286 |
site_id | SWS_FT_FI18 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by CDK1 and PKB => ECO:0000269|PubMed:26440888, ECO:0000269|PubMed:32351706, ECO:0000269|PubMed:33542149 |
Chain | Residue | Details |
K | SER305 |
site_id | SWS_FT_FI19 |
Number of Residues | 1 |
Details | MOD_RES: 5-glutamyl glutamate => ECO:0000250|UniProtKB:Q8C6L5 |
Chain | Residue | Details |
K | GLU314 |
site_id | SWS_FT_FI20 |
Number of Residues | 3 |
Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:30799039 |
Chain | Residue | Details |
K | LYS384 | |
K | LYS392 | |
K | LYS394 |
site_id | SWS_FT_FI21 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:30799039, ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
K | LYS414 |
site_id | SWS_FT_FI22 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:32474700 |
Chain | Residue | Details |
K | SER434 | |
K | SER435 |
site_id | SWS_FT_FI23 |
Number of Residues | 2 |
Details | MOD_RES: (Microbial infection) Deamidated glutamine; by herpes simplex virus 1/HHV-1 UL37 => ECO:0000269|PubMed:30092200 |
Chain | Residue | Details |
K | GLN451 | |
K | GLN454 |
site_id | SWS_FT_FI24 |
Number of Residues | 1 |
Details | MOD_RES: N6-methyllysine => ECO:0000269|PubMed:35210392 |
Chain | Residue | Details |
K | LYS506 |
site_id | SWS_FT_FI25 |
Number of Residues | 2 |
Details | LIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:37802025 |
Chain | Residue | Details |
K | CYS404 | |
K | CYS405 |
site_id | SWS_FT_FI26 |
Number of Residues | 1 |
Details | LIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:35438208 |
Chain | Residue | Details |
K | CYS474 |
site_id | SWS_FT_FI27 |
Number of Residues | 1 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:28273161 |
Chain | Residue | Details |
K | LYS173 |
site_id | SWS_FT_FI28 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:27637147 |
Chain | Residue | Details |
K | LYS479 |
site_id | SWS_FT_FI29 |
Number of Residues | 1 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269|PubMed:27637147 |
Chain | Residue | Details |
K | LYS231 |
site_id | SWS_FT_FI30 |
Number of Residues | 1 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:27637147 |
Chain | Residue | Details |
K | LYS285 |
site_id | SWS_FT_FI31 |
Number of Residues | 1 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:Q8C6L5 |
Chain | Residue | Details |
K | LYS347 |
site_id | SWS_FT_FI32 |
Number of Residues | 1 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:28273161 |
Chain | Residue | Details |
K | LYS384 |
site_id | SWS_FT_FI33 |
Number of Residues | 1 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000250|UniProtKB:Q8C6L5 |
Chain | Residue | Details |
K | LYS394 |
site_id | SWS_FT_FI34 |
Number of Residues | 1 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:35503863 |
Chain | Residue | Details |
K | LYS411 |
site_id | SWS_FT_FI35 |
Number of Residues | 1 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:27666593 |
Chain | Residue | Details |
K | LYS414 |
site_id | SWS_FT_FI36 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:38418882 |
Chain | Residue | Details |
K | LYS427 | |
K | LYS428 |