eF-site ID 5gs5-ABCD PDB Code 5gs5 Chain A, B, C, D click to enlarge Title Crystal structure of apo rat STING Classification IMMUNE SYSTEM Compound Stimulator of interferon genes protein Source Rattus norvegicus (Rat) (STING_RAT) Sequence A:  GSHMAPAEVSAVCEEKNFNVAHGLAWSYYIGYLKLILPGL QARIRMFNQLHNNMLSGAGSRRLYILFPLDCGVPDDLSVA DPNIRFRDMLPQQNTDRAGVKNRAYSNSVYELLENGQPAG ACILEYATPLQTLFAMSQDGKAGFSREDRLEQAKLFCRTL EEILADVPESRNHCRLIVYQESEEGNSFSLSQEVLRHIRQ B:  SHMAPAEVSAVCEEKNFNVAHGLAWSYYIGYLKLILPGLQ ARIRMFNQLHNNMLSGAGSRRLYILFPLDCGVPDDLSVAD PNIRFRDMLPQQNTDRAGVKNRAYSNSVYELLENGQPAGA CILEYATPLQTLFAMSQDGKAGFSREDRLEQAKLFCRTLE EILADVPESRNHCRLIVYQESEEGNSFSLSQEVLRHIRQE EAAAA C:  HSSGENLYFQGSHMAPAEVSAVCEEKNFNVAHGLAWSYYI GYLKLILPGLQARIRMFNQLHNNMLSGAGSRRLYILFPLD CGVPDDLSVADPNIRFRDMLPQQNTDRAGVKNRAYSNSVY ELLENGQPAGACILEYATPLQTLFAMSQDGKAGFSREDRL EQAKLFCRTLEEILADVPESRNHCRLIVYQESEEGNSFSL SQEVLRHIRQEEAAAA D:  SSGENLYFQGSHMAPAEVSAVCEEKNFNVAHGLAWSYYIG YLKLILPGLQARIRMFNQLHNNMLSGAGSRRLYILFPLDC GVPDDLSVADPNIRFRDMLPQQNTDRAGVKNRAYSNSVYE LLENGQPAGACILEYATPLQTLFAMSQDGKAGFSREDRLE QAKLFCRTLEEILADVPESRNHCRLIVYQESEEGNSFSLS QEVLRHIRQEEAA Description Functional site 1) chain A residue 176 type sequence Q description binding site for residue SO4 A 401 source : AC1 2) chain A residue 180 type sequence R description binding site for residue SO4 A 401 source : AC1 3) chain A residue 306 type sequence R description binding site for residue SO4 A 401 source : AC1 4) chain D residue 174 type sequence G description binding site for residue SO4 A 401 source : AC1 5) chain D residue 176 type sequence Q description binding site for residue SO4 A 401 source : AC1 6) chain D residue 177 type sequence A description binding site for residue SO4 A 401 source : AC1 7) chain D residue 180 type sequence R description binding site for residue SO4 A 401 source : AC1 8) chain D residue 232 type sequence R description binding site for residue SO4 A 401 source : AC1 9) chain A residue 180 type sequence R description binding site for residue SO4 A 402 source : AC2 10) chain D residue 173 type sequence P description binding site for residue SO4 A 402 source : AC2 11) chain D residue 174 type sequence G description binding site for residue SO4 A 402 source : AC2 12) chain D residue 232 type sequence R description binding site for residue SO4 A 402 source : AC2 13) chain D residue 305 type sequence S description binding site for residue SO4 A 402 source : AC2 14) chain D residue 306 type sequence R description binding site for residue SO4 A 402 source : AC2 15) chain D residue 308 type sequence H description binding site for residue SO4 A 402 source : AC2 16) chain B residue 193 type sequence A description binding site for residue SO4 B 401 source : AC3 17) chain B residue 196 type sequence R description binding site for residue SO4 B 401 source : AC3 18) chain B residue 197 type sequence R description binding site for residue SO4 B 401 source : AC3 19) chain B residue 340 type sequence A description binding site for residue SO4 B 401 source : AC3 20) chain C residue 180 type sequence R description binding site for residue SO4 B 401 source : AC3 21) chain B residue 176 type sequence Q description binding site for residue SO4 C 401 source : AC4 22) chain B residue 180 type sequence R description binding site for residue SO4 C 401 source : AC4 23) chain B residue 306 type sequence R description binding site for residue SO4 C 401 source : AC4 24) chain C residue 174 type sequence G description binding site for residue SO4 C 401 source : AC4 25) chain C residue 176 type sequence Q description binding site for residue SO4 C 401 source : AC4 26) chain C residue 177 type sequence A description binding site for residue SO4 C 401 source : AC4 27) chain C residue 180 type sequence R description binding site for residue SO4 C 401 source : AC4 28) chain C residue 232 type sequence R description binding site for residue SO4 C 401 source : AC4 29) chain B residue 180 type sequence R description binding site for residue SO4 C 402 source : AC5 30) chain C residue 173 type sequence P description binding site for residue SO4 C 402 source : AC5 31) chain C residue 174 type sequence G description binding site for residue SO4 C 402 source : AC5 32) chain C residue 232 type sequence R description binding site for residue SO4 C 402 source : AC5 33) chain C residue 306 type sequence R description binding site for residue SO4 C 402 source : AC5 34) chain C residue 308 type sequence H description binding site for residue SO4 C 402 source : AC5 35) chain A residue 227 type sequence Q description binding site for residue SO4 C 403 source : AC6 36) chain C residue 157 type sequence H description binding site for residue SO4 C 403 source : AC6 37) chain C residue 161 type sequence W description binding site for residue SO4 C 403 source : AC6 38) chain A residue 334 type sequence R description binding site for residue SO4 D 401 source : AC7 39) chain D residue 220 type sequence R description binding site for residue SO4 D 401 source : AC7 40) chain D residue 222 type sequence R description binding site for residue SO4 D 401 source : AC7 41) chain A residue 228 type sequence Q description binding site for residue SO4 D 402 source : AC8 42) chain A residue 230 type sequence T description binding site for residue SO4 D 402 source : AC8 43) chain A residue 232 type sequence R description binding site for residue SO4 D 402 source : AC8 44) chain D residue 232 type sequence R description binding site for residue SO4 D 402 source : AC8 45) chain D residue 233 type sequence A description binding site for residue SO4 D 402 source : AC8 46) chain D residue 234 type sequence G description binding site for residue SO4 D 402 source : AC8 47) chain B residue 227 type sequence Q description binding site for residue SO4 D 403 source : AC9 48) chain D residue 157 type sequence H description binding site for residue SO4 D 403 source : AC9 49) chain D residue 161 type sequence W description binding site for residue SO4 D 403 source : AC9 50) chain A residue 241 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q86WV6 source Swiss-Prot : SWS_FT_FI4 51) chain B residue 241 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q86WV6 source Swiss-Prot : SWS_FT_FI4 52) chain C residue 241 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q86WV6 source Swiss-Prot : SWS_FT_FI4 53) chain D residue 241 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q86WV6 source Swiss-Prot : SWS_FT_FI4 54) chain A residue 162 type BINDING sequence S description BINDING => ECO:0000305|PubMed:26669264 source Swiss-Prot : SWS_FT_FI1 55) chain B residue 162 type BINDING sequence S description BINDING => ECO:0000305|PubMed:26669264 source Swiss-Prot : SWS_FT_FI1 56) chain C residue 162 type BINDING sequence S description BINDING => ECO:0000305|PubMed:26669264 source Swiss-Prot : SWS_FT_FI1 57) chain D residue 162 type BINDING sequence S description BINDING => ECO:0000305|PubMed:26669264 source Swiss-Prot : SWS_FT_FI1 58) chain A residue 151 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:Q3TBT3 source Swiss-Prot : SWS_FT_FI5 59) chain B residue 151 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:Q3TBT3 source Swiss-Prot : SWS_FT_FI5 60) chain C residue 151 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:Q3TBT3 source Swiss-Prot : SWS_FT_FI5 61) chain D residue 151 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:Q3TBT3 source Swiss-Prot : SWS_FT_FI5 62) chain A residue 236 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:Q86WV6 source Swiss-Prot : SWS_FT_FI6 63) chain B residue 236 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:Q86WV6 source Swiss-Prot : SWS_FT_FI6 64) chain C residue 236 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:Q86WV6 source Swiss-Prot : SWS_FT_FI6 65) chain D residue 236 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:Q86WV6 source Swiss-Prot : SWS_FT_FI6 66) chain A residue 166 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q3TBT3 source Swiss-Prot : SWS_FT_FI2 67) chain A residue 263 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:Q3TBT3 source Swiss-Prot : SWS_FT_FI2 68) chain B residue 166 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q3TBT3 source Swiss-Prot : SWS_FT_FI2 69) chain B residue 263 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:Q3TBT3 source Swiss-Prot : SWS_FT_FI2 70) chain C residue 166 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q3TBT3 source Swiss-Prot : SWS_FT_FI2 71) chain C residue 263 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:Q3TBT3 source Swiss-Prot : SWS_FT_FI2 72) chain D residue 166 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q3TBT3 source Swiss-Prot : SWS_FT_FI2 73) chain D residue 263 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:Q3TBT3 source Swiss-Prot : SWS_FT_FI2 74) chain A residue 167 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:Q86WV6 source Swiss-Prot : SWS_FT_FI3 75) chain A residue 238 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:Q86WV6 source Swiss-Prot : SWS_FT_FI3 76) chain B residue 167 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:Q86WV6 source Swiss-Prot : SWS_FT_FI3 77) chain B residue 238 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:Q86WV6 source Swiss-Prot : SWS_FT_FI3 78) chain C residue 167 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:Q86WV6 source Swiss-Prot : SWS_FT_FI3 79) chain C residue 238 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:Q86WV6 source Swiss-Prot : SWS_FT_FI3 80) chain D residue 167 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:Q86WV6 source Swiss-Prot : SWS_FT_FI3 81) chain D residue 238 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:Q86WV6 source Swiss-Prot : SWS_FT_FI3

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