eF-site ID 3jad-ABCDE PDB Code 3jad Chain A, B, C, D, E click to enlarge Title Structure of alpha-1 glycine receptor by single particle electron cryo-microscopy, strychnine-bound state Classification SIGNALING PROTEIN/ANTAGONIST Compound Glycine receptor subunit alphaZ1 Source (3JAD) Sequence A:  APSEFLDKLMGKVSGYDARIRPNFKGPPVNVTCNIFINSF GSIAETTMDYRVNIFLRQQWNDPRLAYSEYPDDSLDLDPS MLDSIWKPDLFFANEKGANFHEVTTDNKLLRISKNGNVLY SIRITLVLACPMDLKNFPMDVQTCIMQLESFGYTMNDLIF EWDEKGAVQVADGLTLPQFILKEEKDLRYCTKHYNTGKFT CIEARFHLERQMGYYLIQMYIPSLLIVILSWVSFWINMDA APARVGLGITTVLTMTTQSSGSRASLPKVSYVKAIDIWMA VCLLFVFSALLEYAAVNFIARKLFISRAKRIDTVSRVAFP LVFLIFNIFYWITYKLV B:  APSEFLDKLMGKVSGYDARIRPNFKGPPVNVTCNIFINSF GSIAETTMDYRVNIFLRQQWNDPRLAYSEYPDDSLDLDPS MLDSIWKPDLFFANEKGANFHEVTTDNKLLRISKNGNVLY SIRITLVLACPMDLKNFPMDVQTCIMQLESFGYTMNDLIF EWDEKGAVQVADGLTLPQFILKEEKDLRYCTKHYNTGKFT CIEARFHLERQMGYYLIQMYIPSLLIVILSWVSFWINMDA APARVGLGITTVLTMTTQSSGSRASLPKVSYVKAIDIWMA VCLLFVFSALLEYAAVNFIARKLFISRAKRIDTVSRVAFP LVFLIFNIFYWITYKLV C:  APSEFLDKLMGKVSGYDARIRPNFKGPPVNVTCNIFINSF GSIAETTMDYRVNIFLRQQWNDPRLAYSEYPDDSLDLDPS MLDSIWKPDLFFANEKGANFHEVTTDNKLLRISKNGNVLY SIRITLVLACPMDLKNFPMDVQTCIMQLESFGYTMNDLIF EWDEKGAVQVADGLTLPQFILKEEKDLRYCTKHYNTGKFT CIEARFHLERQMGYYLIQMYIPSLLIVILSWVSFWINMDA APARVGLGITTVLTMTTQSSGSRASLPKVSYVKAIDIWMA VCLLFVFSALLEYAAVNFIARKLFISRAKRIDTVSRVAFP LVFLIFNIFYWITYKLV D:  APSEFLDKLMGKVSGYDARIRPNFKGPPVNVTCNIFINSF GSIAETTMDYRVNIFLRQQWNDPRLAYSEYPDDSLDLDPS MLDSIWKPDLFFANEKGANFHEVTTDNKLLRISKNGNVLY SIRITLVLACPMDLKNFPMDVQTCIMQLESFGYTMNDLIF EWDEKGAVQVADGLTLPQFILKEEKDLRYCTKHYNTGKFT CIEARFHLERQMGYYLIQMYIPSLLIVILSWVSFWINMDA APARVGLGITTVLTMTTQSSGSRASLPKVSYVKAIDIWMA VCLLFVFSALLEYAAVNFIARKLFISRAKRIDTVSRVAFP LVFLIFNIFYWITYKLV E:  APSEFLDKLMGKVSGYDARIRPNFKGPPVNVTCNIFINSF GSIAETTMDYRVNIFLRQQWNDPRLAYSEYPDDSLDLDPS MLDSIWKPDLFFANEKGANFHEVTTDNKLLRISKNGNVLY SIRITLVLACPMDLKNFPMDVQTCIMQLESFGYTMNDLIF EWDEKGAVQVADGLTLPQFILKEEKDLRYCTKHYNTGKFT CIEARFHLERQMGYYLIQMYIPSLLIVILSWVSFWINMDA APARVGLGITTVLTMTTQSSGSRASLPKVSYVKAIDIWMA VCLLFVFSALLEYAAVNFIARKLFISRAKRIDTVSRVAFP LVFLIFNIFYWITYKLV Description (1)  zebra fish alpha1 glycine receptor Functional site 1) chain A residue 154-168 type prosite sequence CPMDLKNFPMDVQTC description NEUROTR_ION_CHANNEL Neurotransmitter-gated ion-channels signature. CpMdLknFPmDvqtC source prosite : PS00236 2) chain A residue 239-260 type TRANSMEM sequence YLIQMYIPSLLIVILSWVSFWI description Helical; Name=1 => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI1 3) chain B residue 239-260 type TRANSMEM sequence YLIQMYIPSLLIVILSWVSFWI description Helical; Name=1 => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI1 4) chain C residue 239-260 type TRANSMEM sequence YLIQMYIPSLLIVILSWVSFWI description Helical; Name=1 => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI1 5) chain D residue 239-260 type TRANSMEM sequence YLIQMYIPSLLIVILSWVSFWI description Helical; Name=1 => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI1 6) chain E residue 239-260 type TRANSMEM sequence YLIQMYIPSLLIVILSWVSFWI description Helical; Name=1 => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI1 7) chain A residue 54 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255, ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI10 8) chain B residue 54 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255, ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI10 9) chain C residue 54 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255, ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI10 10) chain D residue 54 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255, ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI10 11) chain E residue 54 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255, ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI10 12) chain A residue 261-265 type TOPO_DOM sequence NMDAA description Cytoplasmic => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI2 13) chain B residue 261-265 type TOPO_DOM sequence NMDAA description Cytoplasmic => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI2 14) chain C residue 261-265 type TOPO_DOM sequence NMDAA description Cytoplasmic => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI2 15) chain D residue 261-265 type TOPO_DOM sequence NMDAA description Cytoplasmic => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI2 16) chain E residue 261-265 type TOPO_DOM sequence NMDAA description Cytoplasmic => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI2 17) chain A residue 266-286 type TRANSMEM sequence PARVGLGITTVLTMTTQSSGS description Helical; Name=2 => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI3 18) chain B residue 266-286 type TRANSMEM sequence PARVGLGITTVLTMTTQSSGS description Helical; Name=2 => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI3 19) chain C residue 266-286 type TRANSMEM sequence PARVGLGITTVLTMTTQSSGS description Helical; Name=2 => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI3 20) chain D residue 266-286 type TRANSMEM sequence PARVGLGITTVLTMTTQSSGS description Helical; Name=2 => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI3 21) chain E residue 266-286 type TRANSMEM sequence PARVGLGITTVLTMTTQSSGS description Helical; Name=2 => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI3 22) chain A residue 287-297 type TOPO_DOM sequence RASLPKVSYVK description Extracellular => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI4 23) chain B residue 287-297 type TOPO_DOM sequence RASLPKVSYVK description Extracellular => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI4 24) chain C residue 287-297 type TOPO_DOM sequence RASLPKVSYVK description Extracellular => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI4 25) chain D residue 287-297 type TOPO_DOM sequence RASLPKVSYVK description Extracellular => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI4 26) chain E residue 287-297 type TOPO_DOM sequence RASLPKVSYVK description Extracellular => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI4 27) chain A residue 298-318 type TRANSMEM sequence AIDIWMAVCLLFVFSALLEYA description Helical; Name=3 => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI5 28) chain B residue 298-318 type TRANSMEM sequence AIDIWMAVCLLFVFSALLEYA description Helical; Name=3 => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI5 29) chain C residue 298-318 type TRANSMEM sequence AIDIWMAVCLLFVFSALLEYA description Helical; Name=3 => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI5 30) chain D residue 298-318 type TRANSMEM sequence AIDIWMAVCLLFVFSALLEYA description Helical; Name=3 => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI5 31) chain E residue 298-318 type TRANSMEM sequence AIDIWMAVCLLFVFSALLEYA description Helical; Name=3 => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI5 32) chain A residue 208 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P23415 source Swiss-Prot : SWS_FT_FI7 33) chain D residue 208 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P23415 source Swiss-Prot : SWS_FT_FI7 34) chain D residue 210 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P23415 source Swiss-Prot : SWS_FT_FI7 35) chain D residue 231 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P23415 source Swiss-Prot : SWS_FT_FI7 36) chain E residue 208 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P23415 source Swiss-Prot : SWS_FT_FI7 37) chain E residue 210 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P23415 source Swiss-Prot : SWS_FT_FI7 38) chain E residue 231 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P23415 source Swiss-Prot : SWS_FT_FI7 39) chain A residue 210 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P23415 source Swiss-Prot : SWS_FT_FI7 40) chain A residue 231 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P23415 source Swiss-Prot : SWS_FT_FI7 41) chain B residue 208 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P23415 source Swiss-Prot : SWS_FT_FI7 42) chain B residue 210 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P23415 source Swiss-Prot : SWS_FT_FI7 43) chain B residue 231 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P23415 source Swiss-Prot : SWS_FT_FI7 44) chain C residue 208 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P23415 source Swiss-Prot : SWS_FT_FI7 45) chain C residue 210 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P23415 source Swiss-Prot : SWS_FT_FI7 46) chain C residue 231 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P23415 source Swiss-Prot : SWS_FT_FI7 47) chain A residue 218 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI8 48) chain B residue 218 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI8 49) chain C residue 218 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI8 50) chain D residue 218 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI8 51) chain E residue 218 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI8 52) chain A residue 277 type SITE sequence L description Important for obstruction of the ion pore in the closed conformation => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI9 53) chain B residue 277 type SITE sequence L description Important for obstruction of the ion pore in the closed conformation => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI9 54) chain C residue 277 type SITE sequence L description Important for obstruction of the ion pore in the closed conformation => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI9 55) chain D residue 277 type SITE sequence L description Important for obstruction of the ion pore in the closed conformation => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI9 56) chain E residue 277 type SITE sequence L description Important for obstruction of the ion pore in the closed conformation => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI9

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