eF-site ID 5vdh-ABCDE PDB Code 5vdh Chain A, B, C, D, E click to enlarge Title Crystal Structure of Human Glycine Receptor alpha-3 Bound to AM-3607, Glycine, and Ivermectin Classification TRANSPORT PROTEIN Compound Glycine receptor subunit alpha-3 Source (GLRA3_HUMAN) Sequence A:  MSPSDFLDKLMGRTSGYDARIRPNFKGPPVNVTCNIFINS FGSIAETTMDYRVNIFLRQKWNDPRLAYSEYPDDSLDLDP SMLDSIWKPDLFFANEKGANFHEVTTDNKLLRIFKNGNVL YSIRLTLTLSCPMDLKNFPMDVQTCIMQLESFGYTMNDLI FEWQDEAPVQVAEGLTLPQFLLKEEKDLRYCTKHYNTGKF TCIEVRFHLERQMGYYLIQMYIPSLLIVILSWVSFWINMD AAPARVALGITTVLTMTTQSSGSRASLPKVSYVKAIDIWM AVCLLFVFSALLEYAAVNFVSRAGTKVFIDRAKKIDTISR ACFPLAFLIFNIFYWVIY B:  APMSPSDFLDKLMGRTSGYDARIRPNFKGPPVNVTCNIFI NSFGSIAETTMDYRVNIFLRQKWNDPRLAYSEYPDDSLDL DPSMLDSIWKPDLFFANEKGANFHEVTTDNKLLRIFKNGN VLYSIRLTLTLSCPMDLKNFPMDVQTCIMQLESFGYTMND LIFEWQDEAPVQVAEGLTLPQFLLKEEKDLRYCTKHYNTG KFTCIEVRFHLERQMGYYLIQMYIPSLLIVILSWVSFWIN MDAAPARVALGITTVLTMTTQSSGSRASLPKVSYVKAIDI WMAVCLLFVFSALLEYAAVNFVSRAGTKVFIDRAKKIDTI SRACFPLAFLIFNIFYWVIYKIL C:  MSPSDFLDKLMGRTSGYDARIRPNFKGPPVNVTCNIFINS FGSIAETTMDYRVNIFLRQKWNDPRLAYSEYPDDSLDLDP SMLDSIWKPDLFFANEKGANFHEVTTDNKLLRIFKNGNVL YSIRLTLTLSCPMDLKNFPMDVQTCIMQLESFGYTMNDLI FEWQDEAPVQVAEGLTLPQFLLKEEKDLRYCTKHYNTGKF TCIEVRFHLERQMGYYLIQMYIPSLLIVILSWVSFWINMD AAPARVALGITTVLTMTTQSSGSRASLPKVSYVKAIDIWM AVCLLFVFSALLEYAAVNFVSRAGTKVFIDRAKKIDTISR ACFPLAFLIFNIFYWVIY D:  SRSAPMSPSDFLDKLMGRTSGYDARIRPNFKGPPVNVTCN IFINSFGSIAETTMDYRVNIFLRQKWNDPRLAYSEYPDDS LDLDPSMLDSIWKPDLFFANEKGANFHEVTTDNKLLRIFK NGNVLYSIRLTLTLSCPMDLKNFPMDVQTCIMQLESFGYT MNDLIFEWQDEAPVQVAEGLTLPQFLLKEEKDLRYCTKHY NTGKFTCIEVRFHLERQMGYYLIQMYIPSLLIVILSWVSF WINMDAAPARVALGITTVLTMTTQSSGSRASLPKVSYVKA IDIWMAVCLLFVFSALLEYAAVNFVSRAGTKVFIDRAKKI DTISRACFPLAFLIFNIFYWVIY E:  MSPSDFLDKLMGRTSGYDARIRPNFKGPPVNVTCNIFINS FGSIAETTMDYRVNIFLRQKWNDPRLAYSEYPDDSLDLDP SMLDSIWKPDLFFANEKGANFHEVTTDNKLLRIFKNGNVL YSIRLTLTLSCPMDLKNFPMDVQTCIMQLESFGYTMNDLI FEWQDEAPVQVAEGLTLPQFLLKEEKDLRYCTKHYNTGKF TCIEVRFHLERQMGYYLIQMYIPSLLIVILSWVSFWINMD AAPARVALGITTVLTMTTQSSGSRASLPKVSYVKAIDIWM AVCLLFVFSALLEYAAVNFVSRAGTKVFIDRAKKIDTISR ACFPLAFLIFNIFYWVIY Description Functional site 1) chain A residue 223-244 type TRANSMEM sequence YLIQMYIPSLLIVILSWVSFWI description Helical; Name=1 => ECO:0000269|PubMed:26416729 source Swiss-Prot : SWS_FT_FI2 2) chain B residue 223-244 type TRANSMEM sequence YLIQMYIPSLLIVILSWVSFWI description Helical; Name=1 => ECO:0000269|PubMed:26416729 source Swiss-Prot : SWS_FT_FI2 3) chain C residue 223-244 type TRANSMEM sequence YLIQMYIPSLLIVILSWVSFWI description Helical; Name=1 => ECO:0000269|PubMed:26416729 source Swiss-Prot : SWS_FT_FI2 4) chain D residue 223-244 type TRANSMEM sequence YLIQMYIPSLLIVILSWVSFWI description Helical; Name=1 => ECO:0000269|PubMed:26416729 source Swiss-Prot : SWS_FT_FI2 5) chain E residue 223-244 type TRANSMEM sequence YLIQMYIPSLLIVILSWVSFWI description Helical; Name=1 => ECO:0000269|PubMed:26416729 source Swiss-Prot : SWS_FT_FI2 6) chain A residue 245-249 type TOPO_DOM sequence NMDAA description Cytoplasmic => ECO:0000269|PubMed:26416729 source Swiss-Prot : SWS_FT_FI3 7) chain B residue 245-249 type TOPO_DOM sequence NMDAA description Cytoplasmic => ECO:0000269|PubMed:26416729 source Swiss-Prot : SWS_FT_FI3 8) chain C residue 245-249 type TOPO_DOM sequence NMDAA description Cytoplasmic => ECO:0000269|PubMed:26416729 source Swiss-Prot : SWS_FT_FI3 9) chain D residue 245-249 type TOPO_DOM sequence NMDAA description Cytoplasmic => ECO:0000269|PubMed:26416729 source Swiss-Prot : SWS_FT_FI3 10) chain E residue 245-249 type TOPO_DOM sequence NMDAA description Cytoplasmic => ECO:0000269|PubMed:26416729 source Swiss-Prot : SWS_FT_FI3 11) chain A residue 250-270 type TRANSMEM sequence PARVALGITTVLTMTTQSSGS description Helical; Name=2 => ECO:0000269|PubMed:26416729 source Swiss-Prot : SWS_FT_FI4 12) chain B residue 250-270 type TRANSMEM sequence PARVALGITTVLTMTTQSSGS description Helical; Name=2 => ECO:0000269|PubMed:26416729 source Swiss-Prot : SWS_FT_FI4 13) chain C residue 250-270 type TRANSMEM sequence PARVALGITTVLTMTTQSSGS description Helical; Name=2 => ECO:0000269|PubMed:26416729 source Swiss-Prot : SWS_FT_FI4 14) chain D residue 250-270 type TRANSMEM sequence PARVALGITTVLTMTTQSSGS description Helical; Name=2 => ECO:0000269|PubMed:26416729 source Swiss-Prot : SWS_FT_FI4 15) chain E residue 250-270 type TRANSMEM sequence PARVALGITTVLTMTTQSSGS description Helical; Name=2 => ECO:0000269|PubMed:26416729 source Swiss-Prot : SWS_FT_FI4 16) chain A residue 282-302 type TRANSMEM sequence AIDIWMAVCLLFVFSALLEYA description Helical; Name=3 => ECO:0000269|PubMed:26416729 source Swiss-Prot : SWS_FT_FI5 17) chain B residue 282-302 type TRANSMEM sequence AIDIWMAVCLLFVFSALLEYA description Helical; Name=3 => ECO:0000269|PubMed:26416729 source Swiss-Prot : SWS_FT_FI5 18) chain C residue 282-302 type TRANSMEM sequence AIDIWMAVCLLFVFSALLEYA description Helical; Name=3 => ECO:0000269|PubMed:26416729 source Swiss-Prot : SWS_FT_FI5 19) chain D residue 282-302 type TRANSMEM sequence AIDIWMAVCLLFVFSALLEYA description Helical; Name=3 => ECO:0000269|PubMed:26416729 source Swiss-Prot : SWS_FT_FI5 20) chain E residue 282-302 type TRANSMEM sequence AIDIWMAVCLLFVFSALLEYA description Helical; Name=3 => ECO:0000269|PubMed:26416729 source Swiss-Prot : SWS_FT_FI5 21) chain A residue 325-345 type TRANSMEM sequence ISRACFPLAFLIFNIFYWVIY description Helical; Name=4 => ECO:0000269|PubMed:26416729 source Swiss-Prot : SWS_FT_FI6 22) chain B residue 325-345 type TRANSMEM sequence ISRACFPLAFLIFNIFYWVIY description Helical; Name=4 => ECO:0000269|PubMed:26416729 source Swiss-Prot : SWS_FT_FI6 23) chain C residue 325-345 type TRANSMEM sequence ISRACFPLAFLIFNIFYWVIY description Helical; Name=4 => ECO:0000269|PubMed:26416729 source Swiss-Prot : SWS_FT_FI6 24) chain D residue 325-345 type TRANSMEM sequence ISRACFPLAFLIFNIFYWVIY description Helical; Name=4 => ECO:0000269|PubMed:26416729 source Swiss-Prot : SWS_FT_FI6 25) chain E residue 325-345 type TRANSMEM sequence ISRACFPLAFLIFNIFYWVIY description Helical; Name=4 => ECO:0000269|PubMed:26416729 source Swiss-Prot : SWS_FT_FI6 26) chain A residue 192 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P23415 source Swiss-Prot : SWS_FT_FI7 27) chain D residue 192 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P23415 source Swiss-Prot : SWS_FT_FI7 28) chain D residue 194 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P23415 source Swiss-Prot : SWS_FT_FI7 29) chain D residue 215 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P23415 source Swiss-Prot : SWS_FT_FI7 30) chain E residue 192 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P23415 source Swiss-Prot : SWS_FT_FI7 31) chain E residue 194 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P23415 source Swiss-Prot : SWS_FT_FI7 32) chain E residue 215 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P23415 source Swiss-Prot : SWS_FT_FI7 33) chain A residue 194 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P23415 source Swiss-Prot : SWS_FT_FI7 34) chain A residue 215 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P23415 source Swiss-Prot : SWS_FT_FI7 35) chain B residue 192 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P23415 source Swiss-Prot : SWS_FT_FI7 36) chain B residue 194 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P23415 source Swiss-Prot : SWS_FT_FI7 37) chain B residue 215 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P23415 source Swiss-Prot : SWS_FT_FI7 38) chain C residue 192 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P23415 source Swiss-Prot : SWS_FT_FI7 39) chain C residue 194 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P23415 source Swiss-Prot : SWS_FT_FI7 40) chain C residue 215 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P23415 source Swiss-Prot : SWS_FT_FI7 41) chain A residue 202 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:26416729 source Swiss-Prot : SWS_FT_FI8 42) chain B residue 202 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:26416729 source Swiss-Prot : SWS_FT_FI8 43) chain C residue 202 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:26416729 source Swiss-Prot : SWS_FT_FI8 44) chain D residue 202 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:26416729 source Swiss-Prot : SWS_FT_FI8 45) chain E residue 202 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:26416729 source Swiss-Prot : SWS_FT_FI8 46) chain A residue 261 type SITE sequence L description Important for obstruction of the ion pore in the closed conformation => ECO:0000269|PubMed:26416729 source Swiss-Prot : SWS_FT_FI9 47) chain B residue 261 type SITE sequence L description Important for obstruction of the ion pore in the closed conformation => ECO:0000269|PubMed:26416729 source Swiss-Prot : SWS_FT_FI9 48) chain C residue 261 type SITE sequence L description Important for obstruction of the ion pore in the closed conformation => ECO:0000269|PubMed:26416729 source Swiss-Prot : SWS_FT_FI9 49) chain D residue 261 type SITE sequence L description Important for obstruction of the ion pore in the closed conformation => ECO:0000269|PubMed:26416729 source Swiss-Prot : SWS_FT_FI9 50) chain E residue 261 type SITE sequence L description Important for obstruction of the ion pore in the closed conformation => ECO:0000269|PubMed:26416729 source Swiss-Prot : SWS_FT_FI9 51) chain E residue 271-281 type TOPO_DOM sequence RASLPKVSYVK description Extracellular => ECO:0000269|PubMed:26416729 source Swiss-Prot : SWS_FT_FI1 52) chain A residue 271-281 type TOPO_DOM sequence RASLPKVSYVK description Extracellular => ECO:0000269|PubMed:26416729 source Swiss-Prot : SWS_FT_FI1 53) chain B residue 271-281 type TOPO_DOM sequence RASLPKVSYVK description Extracellular => ECO:0000269|PubMed:26416729 source Swiss-Prot : SWS_FT_FI1 54) chain C residue 271-281 type TOPO_DOM sequence RASLPKVSYVK description Extracellular => ECO:0000269|PubMed:26416729 source Swiss-Prot : SWS_FT_FI1 55) chain D residue 271-281 type TOPO_DOM sequence RASLPKVSYVK description Extracellular => ECO:0000269|PubMed:26416729 source Swiss-Prot : SWS_FT_FI1 56) chain A residue 138-152 type prosite sequence CPMDLKNFPMDVQTC description NEUROTR_ION_CHANNEL Neurotransmitter-gated ion-channels signature. CpMdLknFPmDvqtC source prosite : PS00236 57) chain A residue 38 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255, ECO:0000269|PubMed:26416729, ECO:0007744|PDB:5CFB source Swiss-Prot : SWS_FT_FI10 58) chain B residue 38 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255, ECO:0000269|PubMed:26416729, ECO:0007744|PDB:5CFB source Swiss-Prot : SWS_FT_FI10 59) chain C residue 38 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255, ECO:0000269|PubMed:26416729, ECO:0007744|PDB:5CFB source Swiss-Prot : SWS_FT_FI10 60) chain D residue 38 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255, ECO:0000269|PubMed:26416729, ECO:0007744|PDB:5CFB source Swiss-Prot : SWS_FT_FI10 61) chain E residue 38 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255, ECO:0000269|PubMed:26416729, ECO:0007744|PDB:5CFB source Swiss-Prot : SWS_FT_FI10

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