eF-site ID 1cju-C PDB Code 1cju Chain C click to enlarge Title COMPLEX OF GS-ALPHA WITH THE CATALYTIC DOMAINS OF MAMMALIAN ADENYLYL CYCLASE: COMPLEX WITH BETA-L-2',3'-DIDEOXYATP AND MG Classification LYASE/LYASE/SIGNALING PROTEIN Compound ADENYLATE CYCLASE, TYPE V Source Canis familiaris (Dog) (Canis lupus familiaris) (GNAS_BOVIN) Sequence C:  ATHRLLLLGAGESGKSTIVKQMRILHVNGEKATKVQDIKN NLKEAIETIVAAMSNLVPPVELANPENQFRVDYILSVMNV PDFDFPPEFYEHAKALWEDEGVRACYERSNEYQLIDCAQY FLDKIDVIKQDDYVPSDQDLLRCRVLTSGIFETKFQVDKV NFHMFDVGGQRDERRKWIQCFNDVTAIIFVVASSSYNMVI REDNQTNRLQEALNLFKSIWNNRWLRTISVILFLNKQDLL AEKVLAGKSKIEDYFPEFARYTTPEDATPEPGEDPRVTRA KYFIRDEFLRISTASGDGRHYCYPHFTCAVDTENIRRVFN DCRDIIQRMHL Description Functional site 1) chain C residue 54 type sequence S description BINDING SITE FOR RESIDUE MG C 403 source : AC1 2) chain C residue 204 type sequence T description BINDING SITE FOR RESIDUE MG C 403 source : AC1 3) chain C residue 51 type sequence S description BINDING SITE FOR RESIDUE CL C 404 source : AC2 4) chain C residue 249 type sequence A description BINDING SITE FOR RESIDUE CL C 404 source : AC2 5) chain C residue 50 type sequence E description BINDING SITE FOR RESIDUE GSP C 405 source : AC5 6) chain C residue 51 type sequence S description BINDING SITE FOR RESIDUE GSP C 405 source : AC5 7) chain C residue 52 type sequence G description BINDING SITE FOR RESIDUE GSP C 405 source : AC5 8) chain C residue 53 type sequence K description BINDING SITE FOR RESIDUE GSP C 405 source : AC5 9) chain C residue 54 type sequence S description BINDING SITE FOR RESIDUE GSP C 405 source : AC5 10) chain C residue 55 type sequence T description BINDING SITE FOR RESIDUE GSP C 405 source : AC5 11) chain C residue 173 type sequence D description BINDING SITE FOR RESIDUE GSP C 405 source : AC5 12) chain C residue 198 type sequence L description BINDING SITE FOR RESIDUE GSP C 405 source : AC5 13) chain C residue 199 type sequence R description BINDING SITE FOR RESIDUE GSP C 405 source : AC5 14) chain C residue 201 type sequence R description BINDING SITE FOR RESIDUE GSP C 405 source : AC5 15) chain C residue 203 type sequence L description BINDING SITE FOR RESIDUE GSP C 405 source : AC5 16) chain C residue 204 type sequence T description BINDING SITE FOR RESIDUE GSP C 405 source : AC5 17) chain C residue 226 type sequence G description BINDING SITE FOR RESIDUE GSP C 405 source : AC5 18) chain C residue 292 type sequence N description BINDING SITE FOR RESIDUE GSP C 405 source : AC5 19) chain C residue 293 type sequence K description BINDING SITE FOR RESIDUE GSP C 405 source : AC5 20) chain C residue 295 type sequence D description BINDING SITE FOR RESIDUE GSP C 405 source : AC5 21) chain C residue 365 type sequence C description BINDING SITE FOR RESIDUE GSP C 405 source : AC5 22) chain C residue 366 type sequence A description BINDING SITE FOR RESIDUE GSP C 405 source : AC5 23) chain C residue 367 type sequence V description BINDING SITE FOR RESIDUE GSP C 405 source : AC5 24) 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 25) chain C residue 198 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 26) chain C residue 224 type BINDING sequence V 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 27) chain C residue 293 type BINDING sequence K 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 28) chain C residue 367 type BINDING sequence V 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 29) 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 30) chain C residue 205 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 31) chain C residue 353 type MOD_RES sequence G description Phosphoserine => ECO:0000250|UniProtKB:P63092 source Swiss-Prot : SWS_FT_FI3 32) chain C residue 301 type CROSSLNK sequence V description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P63092 source Swiss-Prot : SWS_FT_FI6

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