eF-site ID 1azs-ABC PDB Code 1azs Chain A, B, C click to enlarge Title COMPLEX OF GS-ALPHA WITH THE CATALYTIC DOMAINS OF MAMMALIAN ADENYLYL CYCLASE Classification COMPLEX (LYASE/HYDROLASE) Compound VC1 Source Canis familiaris (Dog) (Canis lupus familiaris) (GNAS_BOVIN) Sequence A:  DMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMT LNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADH AHCCVEMGMDMIEAISLVREMTGVNVNMRVGIHSGRVHCG VLGLRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLSY LNGDYEVEPGCGGERNAYLKEHSIETFLIL B:  HQSYDCVCVMFASIPDFKEFYTESDVNKEGLECLRLLNEI IADFDDLLSKPKFSGVEKIKTIGSTYMAATGLSAIRQYMH IGTMVEFAYALVGKLDAINKHSFNDFKLRVGINHGPVIAG VIGAQKPQYDIWGNTVNVASRMDSTGVLDKIQVTEETSLI LQTLGYTCTCRGIINVKGKGDLKTYFVNT C:  VYRATHRLLLLGAGESGKSTIVKQMRILHVNGEKATKVQD IKNNLKEAIETIVAAMSNLVPPVELANPENQFRVDYILSV MNVPDFDFPPEFYEHAKALWEDEGVRACYERSNEYQLIDC AQYFLDKIDVIKQDDYVPSDQDLLRCRVLTSGIFETKFQV DKVNFHMFDVGGQRDERRKWIQCFNDVTAIIFVVASSSYN MVIREDNQTNRLQEALNLFKSIWNNRWLRTISVILFLNKQ DLLAEKVLAGKSKIEDYFPEFARYTTPEDATPEPGEDPRV TRAKYFIRDEFLRISTASGDGRHYCYPHFTCAVDTENIRR VFNDCRDIIQRMHLRQYEL Description Functional site 1) chain A residue 396 type sequence D description MG BINDING SITE IN ACTIVE SITE OF ADENYLYL CYCLASE. source : MGB 2) chain A residue 397 type sequence I description MG BINDING SITE IN ACTIVE SITE OF ADENYLYL CYCLASE. source : MGB 3) chain A residue 440 type sequence D description MG BINDING SITE IN ACTIVE SITE OF ADENYLYL CYCLASE. source : MGB 4) chain C residue 54 type sequence S description BINDING SITE FOR RESIDUE MG C 403 source : AC1 5) chain C residue 204 type sequence T description BINDING SITE FOR RESIDUE MG C 403 source : AC1 6) chain C residue 48 type sequence A description BINDING SITE FOR RESIDUE GSP C 404 source : AC2 7) chain C residue 49 type sequence G description BINDING SITE FOR RESIDUE GSP C 404 source : AC2 8) chain C residue 50 type sequence E description BINDING SITE FOR RESIDUE GSP C 404 source : AC2 9) chain C residue 51 type sequence S description BINDING SITE FOR RESIDUE GSP C 404 source : AC2 10) chain C residue 52 type sequence G description BINDING SITE FOR RESIDUE GSP C 404 source : AC2 11) chain C residue 53 type sequence K description BINDING SITE FOR RESIDUE GSP C 404 source : AC2 12) chain C residue 54 type sequence S description BINDING SITE FOR RESIDUE GSP C 404 source : AC2 13) chain C residue 55 type sequence T description BINDING SITE FOR RESIDUE GSP C 404 source : AC2 14) chain C residue 173 type sequence D description BINDING SITE FOR RESIDUE GSP C 404 source : AC2 15) chain C residue 199 type sequence R description BINDING SITE FOR RESIDUE GSP C 404 source : AC2 16) chain C residue 201 type sequence R description BINDING SITE FOR RESIDUE GSP C 404 source : AC2 17) chain C residue 203 type sequence L description BINDING SITE FOR RESIDUE GSP C 404 source : AC2 18) chain C residue 204 type sequence T description BINDING SITE FOR RESIDUE GSP C 404 source : AC2 19) chain C residue 226 type sequence G description BINDING SITE FOR RESIDUE GSP C 404 source : AC2 20) chain C residue 292 type sequence N description BINDING SITE FOR RESIDUE GSP C 404 source : AC2 21) chain C residue 293 type sequence K description BINDING SITE FOR RESIDUE GSP C 404 source : AC2 22) chain C residue 295 type sequence D description BINDING SITE FOR RESIDUE GSP C 404 source : AC2 23) chain C residue 296 type sequence L description BINDING SITE FOR RESIDUE GSP C 404 source : AC2 24) chain C residue 365 type sequence C description BINDING SITE FOR RESIDUE GSP C 404 source : AC2 25) chain C residue 366 type sequence A description BINDING SITE FOR RESIDUE GSP C 404 source : AC2 26) chain C residue 367 type sequence V description BINDING SITE FOR RESIDUE GSP C 404 source : AC2 27) chain A residue 441 type sequence C description BINDING SITE FOR RESIDUE FKP A 1 source : AC3 28) chain A residue 443 type sequence Y description BINDING SITE FOR RESIDUE FKP A 1 source : AC3 29) chain A residue 506 type sequence V description BINDING SITE FOR RESIDUE FKP A 1 source : AC3 30) chain A residue 507 type sequence W description BINDING SITE FOR RESIDUE FKP A 1 source : AC3 31) chain A residue 508 type sequence S description BINDING SITE FOR RESIDUE FKP A 1 source : AC3 32) chain A residue 511 type sequence V description BINDING SITE FOR RESIDUE FKP A 1 source : AC3 33) chain A residue 512 type sequence T description BINDING SITE FOR RESIDUE FKP A 1 source : AC3 34) chain A residue 515 type sequence N description BINDING SITE FOR RESIDUE FKP A 1 source : AC3 35) chain A residue 518 type sequence E description BINDING SITE FOR RESIDUE FKP A 1 source : AC3 36) chain B residue 896 type sequence K description BINDING SITE FOR RESIDUE FKP A 1 source : AC3 37) chain B residue 940 type sequence I description BINDING SITE FOR RESIDUE FKP A 1 source : AC3 38) chain B residue 941 type sequence G description BINDING SITE FOR RESIDUE FKP A 1 source : AC3 39) chain B residue 942 type sequence S description BINDING SITE FOR RESIDUE FKP A 1 source : AC3 40) chain C residue 300 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P63092 source Swiss-Prot : SWS_FT_FI6 41) chain B residue 1029 type catalytic sequence R description 58 source MCSA : MCSA1 42) chain B residue 1065 type catalytic sequence K description 58 source MCSA : MCSA1 43) chain A residue 440 type catalytic sequence D description 58 source MCSA : MCSA1 44) chain C residue 47 type BINDING sequence G description BINDING => ECO:0000305|PubMed:10427002, ECO:0000305|PubMed:11087399, ECO:0000305|PubMed:15591060, ECO:0000305|PubMed:16766715, ECO:0000305|PubMed:19243146, ECO:0000305|PubMed:9395396, ECO:0000305|PubMed:9417641 source Swiss-Prot : SWS_FT_FI1 45) chain C residue 197 type BINDING sequence L description BINDING => ECO:0000305|PubMed:10427002, ECO:0000305|PubMed:11087399, ECO:0000305|PubMed:15591060, ECO:0000305|PubMed:16766715, ECO:0000305|PubMed:19243146, ECO:0000305|PubMed:9395396, ECO:0000305|PubMed:9417641 source Swiss-Prot : SWS_FT_FI1 46) chain C residue 223 type BINDING sequence D description BINDING => ECO:0000305|PubMed:10427002, ECO:0000305|PubMed:11087399, ECO:0000305|PubMed:15591060, ECO:0000305|PubMed:16766715, ECO:0000305|PubMed:19243146, ECO:0000305|PubMed:9395396, ECO:0000305|PubMed:9417641 source Swiss-Prot : SWS_FT_FI1 47) chain C residue 292 type BINDING sequence N description BINDING => ECO:0000305|PubMed:10427002, ECO:0000305|PubMed:11087399, ECO:0000305|PubMed:15591060, ECO:0000305|PubMed:16766715, ECO:0000305|PubMed:19243146, ECO:0000305|PubMed:9395396, ECO:0000305|PubMed:9417641 source Swiss-Prot : SWS_FT_FI1 48) chain C residue 366 type BINDING sequence A description BINDING => ECO:0000305|PubMed:10427002, ECO:0000305|PubMed:11087399, ECO:0000305|PubMed:15591060, ECO:0000305|PubMed:16766715, ECO:0000305|PubMed:19243146, ECO:0000305|PubMed:9395396, ECO:0000305|PubMed:9417641 source Swiss-Prot : SWS_FT_FI1 49) chain C residue 54 type BINDING sequence S description BINDING => ECO:0000269|PubMed:10427002, ECO:0000269|PubMed:11087399, ECO:0000269|PubMed:15591060, ECO:0000269|PubMed:19243146, ECO:0000269|PubMed:9395396, ECO:0000269|PubMed:9417641, ECO:0000305|PubMed:16766715 source Swiss-Prot : SWS_FT_FI2 50) chain C residue 204 type BINDING sequence T description BINDING => ECO:0000269|PubMed:10427002, ECO:0000269|PubMed:11087399, ECO:0000269|PubMed:15591060, ECO:0000269|PubMed:19243146, ECO:0000269|PubMed:9395396, ECO:0000269|PubMed:9417641, ECO:0000305|PubMed:16766715 source Swiss-Prot : SWS_FT_FI2 51) chain C residue 352 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P63092 source Swiss-Prot : SWS_FT_FI3 52) chain B residue 1008-1031 type prosite sequence GVIGAQKPQYDIWGNTVNVASRMD description GUANYLATE_CYCLASE_1 Guanylate cyclase signature. GVI.GaqkpqYdIWGNTVNvasrmD source prosite : PS00452 53) chain A residue 495-518 type prosite sequence GVLGLRKWQFDVWSNDVTLANHME description GUANYLATE_CYCLASE_1 Guanylate cyclase signature. GVI.GaqkpqYdIWGNTVNvasrmD source prosite : PS00452

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