eF-site ID 1cul-C PDB Code 1cul Chain C click to enlarge Title COMPLEX OF GS-ALPHA WITH THE CATALYTIC DOMAINS OF MAMMALIAN ADENYLYL CYCLASE: COMPLEX WITH 2',5'-DIDEOXY-ADENOSINE 3'-TRIPHOSPHATE AND MG Classification Lyase/Lyase/Signaling protein Compound TYPE V ADENYLYL CYCLASE Source null (GNAS_BOVIN) Sequence C:  ATHRLLLLGAGESGKSTIVKQMRILHVGEKATKVQDIKNN LKEAIETIVAAMSNLVPPVELANPENQFRVDYILSVMNVP DFDFPPEFYEHAKALWEDEGVRACYERSNEYQLIDCAQYF LDKIDVIKQDDYVPSDQDLLRCRVLTSGIFETKFQVDKVN FHMFDVGGQRDERRKWIQCFNDVTAIIFVVASSSYNMVIR EDNQTNRLQEALNLFKSIWNNRWLRTISVILFLNKQDLLA EKVLAGKSKIEDYFPEFARYTTPEDATPEPGEDPRVTRAK YFIRDEFLRISTASGDGRHYCYPHFTCAVDTENIRRVFND CRDIIQRM Description Functional site 1) chain C residue 54 type sequence S description BINDING SITE FOR RESIDUE MG C 396 source : AC3 2) chain C residue 204 type sequence T description BINDING SITE FOR RESIDUE MG C 396 source : AC3 3) chain C residue 51 type sequence S description BINDING SITE FOR RESIDUE CL C 397 source : AC4 4) chain C residue 249 type sequence A description BINDING SITE FOR RESIDUE CL C 397 source : AC4 5) chain C residue 373 type sequence R description BINDING SITE FOR RESIDUE CL C 398 source : AC5 6) chain C residue 373 type sequence R description BINDING SITE FOR RESIDUE CL C 398 source : AC5 7) chain C residue 49 type sequence G description BINDING SITE FOR RESIDUE GSP C 395 source : AC6 8) chain C residue 50 type sequence E description BINDING SITE FOR RESIDUE GSP C 395 source : AC6 9) chain C residue 51 type sequence S description BINDING SITE FOR RESIDUE GSP C 395 source : AC6 10) chain C residue 52 type sequence G description BINDING SITE FOR RESIDUE GSP C 395 source : AC6 11) chain C residue 53 type sequence K description BINDING SITE FOR RESIDUE GSP C 395 source : AC6 12) chain C residue 54 type sequence S description BINDING SITE FOR RESIDUE GSP C 395 source : AC6 13) chain C residue 55 type sequence T description BINDING SITE FOR RESIDUE GSP C 395 source : AC6 14) chain C residue 173 type sequence D description BINDING SITE FOR RESIDUE GSP C 395 source : AC6 15) chain C residue 198 type sequence L description BINDING SITE FOR RESIDUE GSP C 395 source : AC6 16) chain C residue 199 type sequence R description BINDING SITE FOR RESIDUE GSP C 395 source : AC6 17) chain C residue 201 type sequence R description BINDING SITE FOR RESIDUE GSP C 395 source : AC6 18) chain C residue 204 type sequence T description BINDING SITE FOR RESIDUE GSP C 395 source : AC6 19) chain C residue 226 type sequence G description BINDING SITE FOR RESIDUE GSP C 395 source : AC6 20) chain C residue 292 type sequence N description BINDING SITE FOR RESIDUE GSP C 395 source : AC6 21) chain C residue 293 type sequence K description BINDING SITE FOR RESIDUE GSP C 395 source : AC6 22) chain C residue 295 type sequence D description BINDING SITE FOR RESIDUE GSP C 395 source : AC6 23) chain C residue 296 type sequence L description BINDING SITE FOR RESIDUE GSP C 395 source : AC6 24) chain C residue 365 type sequence C description BINDING SITE FOR RESIDUE GSP C 395 source : AC6 25) chain C residue 366 type sequence A description BINDING SITE FOR RESIDUE GSP C 395 source : AC6 26) chain C residue 367 type sequence V description BINDING SITE FOR RESIDUE GSP C 395 source : AC6 27) 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 28) chain C residue 211 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 29) chain C residue 237 type BINDING sequence C 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 30) chain C residue 306 type BINDING sequence S 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 31) chain C residue 380 type BINDING sequence R 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 32) chain C residue 366 type MOD_RES sequence A description Phosphoserine => ECO:0000250|UniProtKB:P63092 source Swiss-Prot : SWS_FT_FI3 33) 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 34) chain C residue 218 type BINDING sequence N 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 35) chain C residue 314 type CROSSLNK sequence E 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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