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1CJU

COMPLEX OF GS-ALPHA WITH THE CATALYTIC DOMAINS OF MAMMALIAN ADENYLYL CYCLASE: COMPLEX WITH BETA-L-2',3'-DIDEOXYATP AND MG

Functional Information from GO Data
ChainGOidnamespacecontents
A0009190biological_processcyclic nucleotide biosynthetic process
A0016849molecular_functionphosphorus-oxygen lyase activity
A0035556biological_processintracellular signal transduction
B0009190biological_processcyclic nucleotide biosynthetic process
B0016849molecular_functionphosphorus-oxygen lyase activity
B0035556biological_processintracellular signal transduction
C0003924molecular_functionGTPase activity
C0005525molecular_functionGTP binding
C0007165biological_processsignal transduction
C0007186biological_processG protein-coupled receptor signaling pathway
C0019001molecular_functionguanyl nucleotide binding
C0031683molecular_functionG-protein beta/gamma-subunit complex binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG C 403
ChainResidue
CSER54
CTHR204
CGSP405
CHOH412
CHOH415

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL C 404
ChainResidue
CSER51
CALA249
CHOH407

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 581
ChainResidue
ADAD102
AASP396
AASP440
AMG582
AHOH57

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 582
ChainResidue
ADAD102
AASP396
AILE397
AASP440
AMG581

site_idAC5
Number of Residues23
DetailsBINDING SITE FOR RESIDUE GSP C 405
ChainResidue
CGLU50
CSER51
CGLY52
CLYS53
CSER54
CTHR55
CASP173
CLEU198
CARG199
CARG201
CLEU203
CTHR204
CGLY226
CASN292
CLYS293
CASP295
CCYS365
CALA366
CVAL367
CMG403
CHOH412
CHOH415
CHOH418

site_idAC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE FOK A 101
ChainResidue
ATYR443
AVAL506
ATRP507
ASER508
AVAL511
ATHR512
AASN515
BHOH17
BPHE895
BILE940
BGLY941
BSER942

site_idAC7
Number of Residues19
DetailsBINDING SITE FOR RESIDUE DAD A 102
ChainResidue
AASP396
AILE397
AGLU398
AGLY399
APHE400
ATHR401
ALEU438
AGLY439
AASP440
AARG484
AMG581
AMG582
BLYS938
BASP1018
BILE1019
BASN1025
BSER1028
BARG1029
BLYS1065

Functional Information from PROSITE/UniProt
site_idPS00452
Number of Residues24
DetailsGUANYLATE_CYCLASE_1 Guanylate cyclase signature. GVI.GaqkpqYdIWGNTVNvasrmD
ChainResidueDetails
BGLY1008-ASP1031
AGLY495-GLU518

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING: 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
ChainResidueDetails
CGLY47
CLEU198
CVAL224
CLYS293
CVAL367

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: 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
ChainResidueDetails
CSER54
CSER205
AGLY521

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P63092
ChainResidueDetails
CGLY353
ALEU565

site_idSWS_FT_FI4
Number of Residues1
DetailsLIPID: N-palmitoyl glycine => ECO:0000269|PubMed:12574119
ChainResidueDetails
CGLY2

site_idSWS_FT_FI5
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:12574119
ChainResidueDetails
CCYS3

site_idSWS_FT_FI6
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P63092
ChainResidueDetails
CVAL301

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ab8
ChainResidueDetails
BARG1029

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ab8
ChainResidueDetails
AHIS516

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1ab8
ChainResidueDetails
CTHR204
CARG201
CGLU50
CGLN227

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ab8
ChainResidueDetails
CGLN227

site_idMCSA1
Number of Residues2
DetailsM-CSA 58
ChainResidueDetails
BARG1029electrostatic stabiliser
BLYS1065electrostatic stabiliser
AGLY521metal ligand

225158

PDB entries from 2024-09-18

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