eF-site ID 1cju-ABC
PDB Code 1cju
Chain A, B, C

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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 A:  MMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMTL
NELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHA
HCCVEMGMDMIEAISLVREMTGVNVNMRVGIHSGRVHCGV
LGLRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLSYL
NGDYEVEPGCGGERNAYLKEHSIETFLIL
B:  YHQSYDCVCVMFASIPDFKEFYTESDVNKEGLECLRLLNE
IIADFDDLLSKPKFSGVEKIKTIGSTYMAATGLSARQYMH
IGTMVEFAYALVGKLDAINKHSFNDFKLRVGINHGPVIAG
VIGAQKPQYDIWGNTVNVASRMDSTGVLDKIQVTEETSLI
LQTLGYTCTCRGIINVKGKGDLKTYFVNT
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 A
residue 396
type
sequence D
description BINDING SITE FOR RESIDUE MG A 581
source : AC3
6) chain A
residue 440
type
sequence D
description BINDING SITE FOR RESIDUE MG A 581
source : AC3
7) chain A
residue 396
type
sequence D
description BINDING SITE FOR RESIDUE MG A 582
source : AC4
8) chain A
residue 397
type
sequence I
description BINDING SITE FOR RESIDUE MG A 582
source : AC4
9) chain A
residue 440
type
sequence D
description BINDING SITE FOR RESIDUE MG A 582
source : AC4
10) chain C
residue 50
type
sequence E
description BINDING SITE FOR RESIDUE GSP C 405
source : AC5
11) chain C
residue 51
type
sequence S
description BINDING SITE FOR RESIDUE GSP C 405
source : AC5
12) chain C
residue 52
type
sequence G
description BINDING SITE FOR RESIDUE GSP C 405
source : AC5
13) chain C
residue 53
type
sequence K
description BINDING SITE FOR RESIDUE GSP C 405
source : AC5
14) chain C
residue 54
type
sequence S
description BINDING SITE FOR RESIDUE GSP C 405
source : AC5
15) chain C
residue 55
type
sequence T
description BINDING SITE FOR RESIDUE GSP C 405
source : AC5
16) chain C
residue 173
type
sequence D
description BINDING SITE FOR RESIDUE GSP C 405
source : AC5
17) chain C
residue 198
type
sequence L
description BINDING SITE FOR RESIDUE GSP C 405
source : AC5
18) chain C
residue 199
type
sequence R
description BINDING SITE FOR RESIDUE GSP C 405
source : AC5
19) chain C
residue 201
type
sequence R
description BINDING SITE FOR RESIDUE GSP C 405
source : AC5
20) chain C
residue 203
type
sequence L
description BINDING SITE FOR RESIDUE GSP C 405
source : AC5
21) chain C
residue 204
type
sequence T
description BINDING SITE FOR RESIDUE GSP C 405
source : AC5
22) chain C
residue 226
type
sequence G
description BINDING SITE FOR RESIDUE GSP C 405
source : AC5
23) chain C
residue 292
type
sequence N
description BINDING SITE FOR RESIDUE GSP C 405
source : AC5
24) chain C
residue 293
type
sequence K
description BINDING SITE FOR RESIDUE GSP C 405
source : AC5
25) chain C
residue 295
type
sequence D
description BINDING SITE FOR RESIDUE GSP C 405
source : AC5
26) chain C
residue 365
type
sequence C
description BINDING SITE FOR RESIDUE GSP C 405
source : AC5
27) chain C
residue 366
type
sequence A
description BINDING SITE FOR RESIDUE GSP C 405
source : AC5
28) chain C
residue 367
type
sequence V
description BINDING SITE FOR RESIDUE GSP C 405
source : AC5
29) chain A
residue 443
type
sequence Y
description BINDING SITE FOR RESIDUE FOK A 101
source : AC6
30) chain A
residue 506
type
sequence V
description BINDING SITE FOR RESIDUE FOK A 101
source : AC6
31) chain A
residue 507
type
sequence W
description BINDING SITE FOR RESIDUE FOK A 101
source : AC6
32) chain A
residue 508
type
sequence S
description BINDING SITE FOR RESIDUE FOK A 101
source : AC6
33) chain A
residue 511
type
sequence V
description BINDING SITE FOR RESIDUE FOK A 101
source : AC6
34) chain A
residue 512
type
sequence T
description BINDING SITE FOR RESIDUE FOK A 101
source : AC6
35) chain A
residue 515
type
sequence N
description BINDING SITE FOR RESIDUE FOK A 101
source : AC6
36) chain B
residue 895
type
sequence F
description BINDING SITE FOR RESIDUE FOK A 101
source : AC6
37) chain B
residue 940
type
sequence I
description BINDING SITE FOR RESIDUE FOK A 101
source : AC6
38) chain B
residue 941
type
sequence G
description BINDING SITE FOR RESIDUE FOK A 101
source : AC6
39) chain B
residue 942
type
sequence S
description BINDING SITE FOR RESIDUE FOK A 101
source : AC6
40) chain A
residue 396
type
sequence D
description BINDING SITE FOR RESIDUE DAD A 102
source : AC7
41) chain A
residue 397
type
sequence I
description BINDING SITE FOR RESIDUE DAD A 102
source : AC7
42) chain A
residue 398
type
sequence E
description BINDING SITE FOR RESIDUE DAD A 102
source : AC7
43) chain A
residue 399
type
sequence G
description BINDING SITE FOR RESIDUE DAD A 102
source : AC7
44) chain A
residue 400
type
sequence F
description BINDING SITE FOR RESIDUE DAD A 102
source : AC7
45) chain A
residue 401
type
sequence T
description BINDING SITE FOR RESIDUE DAD A 102
source : AC7
46) chain A
residue 438
type
sequence L
description BINDING SITE FOR RESIDUE DAD A 102
source : AC7
47) chain A
residue 439
type
sequence G
description BINDING SITE FOR RESIDUE DAD A 102
source : AC7
48) chain A
residue 440
type
sequence D
description BINDING SITE FOR RESIDUE DAD A 102
source : AC7
49) chain A
residue 484
type
sequence R
description BINDING SITE FOR RESIDUE DAD A 102
source : AC7
50) chain B
residue 938
type
sequence K
description BINDING SITE FOR RESIDUE DAD A 102
source : AC7
51) chain B
residue 1018
type
sequence D
description BINDING SITE FOR RESIDUE DAD A 102
source : AC7
52) chain B
residue 1019
type
sequence I
description BINDING SITE FOR RESIDUE DAD A 102
source : AC7
53) chain B
residue 1025
type
sequence N
description BINDING SITE FOR RESIDUE DAD A 102
source : AC7
54) chain B
residue 1028
type
sequence S
description BINDING SITE FOR RESIDUE DAD A 102
source : AC7
55) chain B
residue 1029
type
sequence R
description BINDING SITE FOR RESIDUE DAD A 102
source : AC7
56) chain B
residue 1065
type
sequence K
description BINDING SITE FOR RESIDUE DAD A 102
source : AC7
57) chain B
residue 1029
type catalytic
sequence R
description 58
source MCSA : MCSA1
58) chain B
residue 1065
type catalytic
sequence K
description 58
source MCSA : MCSA1
59) chain A
residue 521
type catalytic
sequence G
description 58
source MCSA : MCSA1
60) 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
61) 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
62) 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
63) 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
64) 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
65) chain C
residue 352
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P63092
source Swiss-Prot : SWS_FT_FI3
66) chain A
residue 565
type MOD_RES
sequence L
description Phosphoserine => ECO:0000250|UniProtKB:P63092
source Swiss-Prot : SWS_FT_FI3
67) chain A
residue 495-518
type prosite
sequence GVLGLRKWQFDVWSNDVTLANHME
description GUANYLATE_CYCLASE_1 Guanylate cyclase signature. GVL.GlrkwqFdVWSNDVTlanhmE
source prosite : PS00452
68) chain B
residue 1008-1031
type prosite
sequence GVIGAQKPQYDIWGNTVNVASRMD
description GUANYLATE_CYCLASE_1 Guanylate cyclase signature. GVL.GlrkwqFdVWSNDVTlanhmE
source prosite : PS00452
69) 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
70) 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
71) chain A
residue 521
type BINDING
sequence G
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
72) 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

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