eF-site ID 3jaf-ABCDE PDB Code 3jaf Chain A, B, C, D, E click to enlarge Title Structure of alpha-1 glycine receptor by single particle electron cryo-microscopy, glycine/ivermectin-bound state Classification SIGNALING PROTEIN Compound Glycine receptor subunit alphaZ1 Source (3JAF) Sequence A:  APSEFLDKLMGKVSGYDARIRPNFKGPPVNVTCNIFINSF GSIAETTMDYRVNIFLRQQWNDPRLAYSEYPDDSLDLDPS MLDSIWKPDLFFANEKGANFHEVTTDNKLLRISKNGNVLY SIRITLVLACPMDLKNFPMDVQTCIMQLESFGYTMNDLIF EWDEKGAVQVADGLTLPQFILKEEKDLRYCTKHYNTGKFT CIEARFHLERQMGYYLIQMYIPSLLIVILSWVSFWINMDA APARVGLGITTVLTMTTQSSGSRASLPKVSYVKAIDIWMA VCLLFVFSALLEYAAVNFIARAGTKLFISRAKRIDTVSRV AFPLVFLIFNIFYWITYKLVPR B:  APSEFLDKLMGKVSGYDARIRPNFKGPPVNVTCNIFINSF GSIAETTMDYRVNIFLRQQWNDPRLAYSEYPDDSLDLDPS MLDSIWKPDLFFANEKGANFHEVTTDNKLLRISKNGNVLY SIRITLVLACPMDLKNFPMDVQTCIMQLESFGYTMNDLIF EWDEKGAVQVADGLTLPQFILKEEKDLRYCTKHYNTGKFT CIEARFHLERQMGYYLIQMYIPSLLIVILSWVSFWINMDA APARVGLGITTVLTMTTQSSGSRASLPKVSYVKAIDIWMA VCLLFVFSALLEYAAVNFIARAGTKLFISRAKRIDTVSRV AFPLVFLIFNIFYWITYKLVPR C:  APSEFLDKLMGKVSGYDARIRPNFKGPPVNVTCNIFINSF GSIAETTMDYRVNIFLRQQWNDPRLAYSEYPDDSLDLDPS MLDSIWKPDLFFANEKGANFHEVTTDNKLLRISKNGNVLY SIRITLVLACPMDLKNFPMDVQTCIMQLESFGYTMNDLIF EWDEKGAVQVADGLTLPQFILKEEKDLRYCTKHYNTGKFT CIEARFHLERQMGYYLIQMYIPSLLIVILSWVSFWINMDA APARVGLGITTVLTMTTQSSGSRASLPKVSYVKAIDIWMA VCLLFVFSALLEYAAVNFIARAGTKLFISRAKRIDTVSRV AFPLVFLIFNIFYWITYKLVPR D:  APSEFLDKLMGKVSGYDARIRPNFKGPPVNVTCNIFINSF GSIAETTMDYRVNIFLRQQWNDPRLAYSEYPDDSLDLDPS MLDSIWKPDLFFANEKGANFHEVTTDNKLLRISKNGNVLY SIRITLVLACPMDLKNFPMDVQTCIMQLESFGYTMNDLIF EWDEKGAVQVADGLTLPQFILKEEKDLRYCTKHYNTGKFT CIEARFHLERQMGYYLIQMYIPSLLIVILSWVSFWINMDA APARVGLGITTVLTMTTQSSGSRASLPKVSYVKAIDIWMA VCLLFVFSALLEYAAVNFIARAGTKLFISRAKRIDTVSRV AFPLVFLIFNIFYWITYKLVPR E:  APSEFLDKLMGKVSGYDARIRPNFKGPPVNVTCNIFINSF GSIAETTMDYRVNIFLRQQWNDPRLAYSEYPDDSLDLDPS MLDSIWKPDLFFANEKGANFHEVTTDNKLLRISKNGNVLY SIRITLVLACPMDLKNFPMDVQTCIMQLESFGYTMNDLIF EWDEKGAVQVADGLTLPQFILKEEKDLRYCTKHYNTGKFT CIEARFHLERQMGYYLIQMYIPSLLIVILSWVSFWINMDA APARVGLGITTVLTMTTQSSGSRASLPKVSYVKAIDIWMA VCLLFVFSALLEYAAVNFIARAGTKLFISRAKRIDTVSRV AFPLVFLIFNIFYWITYKLVPR 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 261-265 type TOPO_DOM sequence NMDAA description Cytoplasmic => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI2 8) chain B residue 261-265 type TOPO_DOM sequence NMDAA description Cytoplasmic => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI2 9) chain C residue 261-265 type TOPO_DOM sequence NMDAA description Cytoplasmic => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI2 10) chain D residue 261-265 type TOPO_DOM sequence NMDAA description Cytoplasmic => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI2 11) chain E residue 261-265 type TOPO_DOM sequence NMDAA description Cytoplasmic => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI2 12) chain A residue 266-286 type TRANSMEM sequence PARVGLGITTVLTMTTQSSGS description Helical; Name=2 => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI3 13) chain B residue 266-286 type TRANSMEM sequence PARVGLGITTVLTMTTQSSGS description Helical; Name=2 => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI3 14) chain C residue 266-286 type TRANSMEM sequence PARVGLGITTVLTMTTQSSGS description Helical; Name=2 => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI3 15) chain D residue 266-286 type TRANSMEM sequence PARVGLGITTVLTMTTQSSGS description Helical; Name=2 => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI3 16) chain E residue 266-286 type TRANSMEM sequence PARVGLGITTVLTMTTQSSGS description Helical; Name=2 => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI3 17) chain A residue 287-297 type TOPO_DOM sequence RASLPKVSYVK description Extracellular => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI4 18) chain B residue 287-297 type TOPO_DOM sequence RASLPKVSYVK description Extracellular => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI4 19) chain C residue 287-297 type TOPO_DOM sequence RASLPKVSYVK description Extracellular => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI4 20) chain D residue 287-297 type TOPO_DOM sequence RASLPKVSYVK description Extracellular => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI4 21) chain E residue 287-297 type TOPO_DOM sequence RASLPKVSYVK description Extracellular => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI4 22) chain A residue 298-318 type TRANSMEM sequence AIDIWMAVCLLFVFSALLEYA description Helical; Name=3 => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI5 23) chain B residue 298-318 type TRANSMEM sequence AIDIWMAVCLLFVFSALLEYA description Helical; Name=3 => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI5 24) chain C residue 298-318 type TRANSMEM sequence AIDIWMAVCLLFVFSALLEYA description Helical; Name=3 => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI5 25) chain D residue 298-318 type TRANSMEM sequence AIDIWMAVCLLFVFSALLEYA description Helical; Name=3 => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI5 26) chain E residue 298-318 type TRANSMEM sequence AIDIWMAVCLLFVFSALLEYA description Helical; Name=3 => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI5 27) chain A residue 208 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P23415 source Swiss-Prot : SWS_FT_FI7 28) chain D residue 208 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P23415 source Swiss-Prot : SWS_FT_FI7 29) chain D residue 210 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P23415 source Swiss-Prot : SWS_FT_FI7 30) chain D residue 231 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P23415 source Swiss-Prot : SWS_FT_FI7 31) chain E residue 208 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P23415 source Swiss-Prot : SWS_FT_FI7 32) chain E residue 210 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P23415 source Swiss-Prot : SWS_FT_FI7 33) chain E residue 231 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P23415 source Swiss-Prot : SWS_FT_FI7 34) chain A residue 210 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P23415 source Swiss-Prot : SWS_FT_FI7 35) chain A residue 231 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P23415 source Swiss-Prot : SWS_FT_FI7 36) chain B residue 208 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P23415 source Swiss-Prot : SWS_FT_FI7 37) chain B residue 210 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P23415 source Swiss-Prot : SWS_FT_FI7 38) chain B residue 231 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P23415 source Swiss-Prot : SWS_FT_FI7 39) chain C residue 208 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P23415 source Swiss-Prot : SWS_FT_FI7 40) chain C residue 210 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P23415 source Swiss-Prot : SWS_FT_FI7 41) chain C residue 231 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P23415 source Swiss-Prot : SWS_FT_FI7 42) chain A residue 218 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI8 43) chain B residue 218 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI8 44) chain C residue 218 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI8 45) chain D residue 218 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI8 46) chain E residue 218 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:26344198 source Swiss-Prot : SWS_FT_FI8 47) 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 48) 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 49) 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 50) 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 51) 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 52) 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 53) 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 54) 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 55) 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 56) 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

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