7CCR
Structure of the 2:2 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 |
| L | 0000786 | cellular_component | nucleosome |
| L | 0003677 | molecular_function | DNA binding |
| L | 0030527 | molecular_function | structural constituent of chromatin |
| L | 0046982 | molecular_function | protein heterodimerization activity |
| M | 0003677 | molecular_function | DNA binding |
| M | 0030527 | molecular_function | structural constituent of chromatin |
| M | 0046982 | molecular_function | protein heterodimerization activity |
| N | 0000786 | cellular_component | nucleosome |
| N | 0003677 | molecular_function | DNA binding |
| N | 0030527 | molecular_function | structural constituent of chromatin |
| N | 0046982 | molecular_function | protein heterodimerization activity |
| O | 0000786 | cellular_component | nucleosome |
| O | 0003677 | molecular_function | DNA binding |
| O | 0030527 | molecular_function | structural constituent of chromatin |
| O | 0046982 | molecular_function | protein heterodimerization activity |
| P | 0000786 | cellular_component | nucleosome |
| P | 0003677 | molecular_function | DNA binding |
| P | 0030527 | molecular_function | structural constituent of chromatin |
| P | 0046982 | molecular_function | protein heterodimerization activity |
| Q | 0003677 | molecular_function | DNA binding |
| Q | 0030527 | molecular_function | structural constituent of chromatin |
| Q | 0046982 | molecular_function | protein heterodimerization activity |
| R | 0000786 | cellular_component | nucleosome |
| R | 0003677 | molecular_function | DNA binding |
| R | 0030527 | molecular_function | structural constituent of chromatin |
| R | 0046982 | molecular_function | protein heterodimerization activity |
| S | 0000786 | cellular_component | nucleosome |
| S | 0003677 | molecular_function | DNA binding |
| S | 0030527 | molecular_function | structural constituent of chromatin |
| S | 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 | 12 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 |
| Chain | Residue | Details |
| B | LYS31 | |
| Q | LYS31 | |
| Q | LYS77 | |
| Q | LYS91 | |
| B | LYS77 | |
| B | LYS91 | |
| F | LYS31 | |
| F | LYS77 | |
| F | LYS91 | |
| M | LYS31 | |
| M | LYS77 | |
| M | LYS91 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-propionyllysine; alternate => ECO:0000269|PubMed:17267393 |
| Chain | Residue | Details |
| B | LYS44 | |
| F | LYS44 | |
| M | LYS44 | |
| Q | LYS44 | |
| V | SER380 | |
| V | LYS414 | |
| R | LYS74 | |
| R | LYS75 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| 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 | |
| M | SER47 | |
| Q | SER47 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455, ECO:0007744|PubMed:20068231 |
| Chain | Residue | Details |
| B | TYR51 | |
| F | TYR51 | |
| M | TYR51 | |
| Q | TYR51 | |
| O | LYS43 | |
| O | LYS85 | |
| S | LYS43 | |
| S | LYS85 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-glutaryllysine; alternate => ECO:0000269|PubMed:31542297 |
| Chain | Residue | Details |
| B | LYS59 | |
| F | LYS59 | |
| M | LYS59 | |
| Q | LYS59 | |
| O | LYS46 | |
| O | LYS108 | |
| S | LYS46 | |
| S | LYS108 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62806 |
| Chain | Residue | Details |
| B | LYS79 | |
| F | LYS79 | |
| M | LYS79 | |
| Q | LYS79 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P62806 |
| Chain | Residue | Details |
| B | THR80 | |
| F | THR80 | |
| M | THR80 | |
| Q | THR80 | |
| V | CYS397 | |
| V | CYS404 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| B | TYR88 | |
| F | TYR88 | |
| M | TYR88 | |
| Q | TYR88 | |
| O | ARG86 | |
| O | ARG92 | |
| S | ARG86 | |
| S | ARG92 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| 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 | |
| M | LYS31 | |
| Q | LYS31 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 8 |
| 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 | |
| V | LYS187 | |
| F | LYS91 | |
| M | LYS91 | |
| Q | LYS91 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 8 |
| 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 | |
| M | LYS59 | |
| M | LYS79 | |
| Q | LYS59 | |
| Q | LYS79 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | SITE: Cleavage; by CASP3 => ECO:0000269|PubMed:30878284 |
| Chain | Residue | Details |
| K | ASP319 | |
| V | ASP319 | |
| H | LYS120 | |
| O | LYS120 | |
| S | LYS120 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | MOD_RES: PolyADP-ribosyl aspartic acid => ECO:0000269|PubMed:35460603 |
| Chain | Residue | Details |
| K | ASP191 | |
| V | ASP191 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 4 |
| 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 | |
| V | ASN210 | |
| V | ASN389 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:33273464 |
| Chain | Residue | Details |
| K | SER213 | |
| V | SER213 |
| site_id | SWS_FT_FI16 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine; by BLK => ECO:0000269|PubMed:30356214 |
| Chain | Residue | Details |
| K | TYR215 | |
| V | TYR215 |
| site_id | SWS_FT_FI17 |
| Number of Residues | 2 |
| Details | MOD_RES: 5-glutamyl polyglutamate => ECO:0000250|UniProtKB:Q8C6L5 |
| Chain | Residue | Details |
| K | GLU286 | |
| V | GLU286 |
| site_id | SWS_FT_FI18 |
| Number of Residues | 2 |
| 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 | |
| V | SER305 |
| site_id | SWS_FT_FI19 |
| Number of Residues | 2 |
| Details | MOD_RES: 5-glutamyl glutamate => ECO:0000250|UniProtKB:Q8C6L5 |
| Chain | Residue | Details |
| K | GLU314 | |
| V | GLU314 |
| site_id | SWS_FT_FI20 |
| Number of Residues | 6 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:30799039 |
| Chain | Residue | Details |
| K | LYS384 | |
| K | LYS392 | |
| K | LYS394 | |
| V | LYS384 | |
| V | LYS392 | |
| V | LYS394 |
| site_id | SWS_FT_FI21 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:30799039, ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| K | LYS414 | |
| V | LYS414 |
| site_id | SWS_FT_FI22 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:32474700 |
| Chain | Residue | Details |
| K | SER434 | |
| K | SER435 | |
| V | SER434 | |
| V | SER435 |
| site_id | SWS_FT_FI23 |
| Number of Residues | 4 |
| 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 | |
| V | GLN451 | |
| V | GLN454 |
| site_id | SWS_FT_FI24 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-methyllysine => ECO:0000269|PubMed:35210392 |
| Chain | Residue | Details |
| K | LYS506 | |
| V | LYS506 |
| site_id | SWS_FT_FI25 |
| Number of Residues | 4 |
| Details | LIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:37802025 |
| Chain | Residue | Details |
| K | CYS404 | |
| K | CYS405 | |
| V | CYS404 | |
| V | CYS405 |
| site_id | SWS_FT_FI26 |
| Number of Residues | 2 |
| Details | LIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:35438208 |
| Chain | Residue | Details |
| K | CYS474 | |
| V | CYS474 |
| site_id | SWS_FT_FI27 |
| Number of Residues | 2 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:28273161 |
| Chain | Residue | Details |
| K | LYS173 | |
| V | LYS173 |
| site_id | SWS_FT_FI28 |
| Number of Residues | 4 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:27637147 |
| Chain | Residue | Details |
| K | LYS479 | |
| V | LYS479 |
| site_id | SWS_FT_FI29 |
| 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 | LYS231 | |
| V | LYS231 |
| site_id | SWS_FT_FI30 |
| Number of Residues | 2 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:27637147 |
| Chain | Residue | Details |
| K | LYS285 | |
| V | LYS285 |
| site_id | SWS_FT_FI31 |
| Number of Residues | 2 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:Q8C6L5 |
| Chain | Residue | Details |
| K | LYS347 | |
| V | LYS347 |
| site_id | SWS_FT_FI32 |
| Number of Residues | 2 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:28273161 |
| Chain | Residue | Details |
| K | LYS384 | |
| V | LYS384 |
| site_id | SWS_FT_FI33 |
| Number of Residues | 2 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000250|UniProtKB:Q8C6L5 |
| Chain | Residue | Details |
| K | LYS394 | |
| V | LYS394 |
| site_id | SWS_FT_FI34 |
| Number of Residues | 2 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:35503863 |
| Chain | Residue | Details |
| K | LYS411 | |
| V | LYS411 |
| site_id | SWS_FT_FI35 |
| Number of Residues | 2 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:27666593 |
| Chain | Residue | Details |
| K | LYS414 | |
| V | LYS414 |
| site_id | SWS_FT_FI36 |
| 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 | LYS427 | |
| K | LYS428 | |
| V | LYS427 | |
| V | LYS428 |
