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2GVZ

Crystal Structure of Complex of Gs- with The Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with MANT-ATP and Mn

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
C0005159molecular_functioninsulin-like growth factor receptor binding
C0005525molecular_functionGTP binding
C0005737cellular_componentcytoplasm
C0005834cellular_componentheterotrimeric G-protein complex
C0005886cellular_componentplasma membrane
C0007165biological_processsignal transduction
C0007186biological_processG protein-coupled receptor signaling pathway
C0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
C0007191biological_processadenylate cyclase-activating dopamine receptor signaling pathway
C0007606biological_processsensory perception of chemical stimulus
C0010856molecular_functionadenylate cyclase activator activity
C0016020cellular_componentmembrane
C0016787molecular_functionhydrolase activity
C0019001molecular_functionguanyl nucleotide binding
C0031683molecular_functionG-protein beta/gamma-subunit complex binding
C0031698molecular_functionbeta-2 adrenergic receptor binding
C0031748molecular_functionD1 dopamine receptor binding
C0031852molecular_functionmu-type opioid receptor binding
C0035255molecular_functionionotropic glutamate receptor binding
C0046872molecular_functionmetal ion binding
C0051430molecular_functioncorticotropin-releasing hormone receptor 1 binding
C0071880biological_processadenylate cyclase-activating adrenergic receptor signaling pathway
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MN C 396
ChainResidue
CSER54
CTHR204
CASP223
CGSP395

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL C 397
ChainResidue
CALA48
CVAL248
CALA249
CARG265
CALA269

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MN A 581
ChainResidue
AONA100
AASP440

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MN A 582
ChainResidue
AONA100
AASP396
AILE397
AASP440

site_idAC5
Number of Residues23
DetailsBINDING SITE FOR RESIDUE GSP C 395
ChainResidue
CGLU50
CSER51
CGLY52
CLYS53
CSER54
CTHR55
CASP173
CLEU198
CARG199
CARG201
CVAL202
CLEU203
CTHR204
CVAL224
CGLY226
CASN292
CLYS293
CASP295
CLEU296
CCYS365
CALA366
CVAL367
CMN396

site_idAC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE FKP A 1
ChainResidue
APHE394
ACYS441
AVAL506
ATRP507
ASER508
AVAL511
ATHR512
AGLU518
BLYS896
BILE940
BSER942
BTHR943

site_idAC7
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ONA A 100
ChainResidue
AASP396
AILE397
AGLY399
APHE400
ATHR401
AALA404
AGLY439
AASP440
AARG484
AMN581
AMN582
BASN1022
BASN1025

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305|PubMed:10427002
ChainResidueDetails
AASP396
AILE397
AASP440
CASN292
CALA366

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:10427002, ECO:0000305|PubMed:11087399, ECO:0000305|PubMed:16766715, ECO:0000305|PubMed:19243146
ChainResidueDetails
ALEU438
AARG484

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P63092
ChainResidueDetails
CSER352

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
CLYS300

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 58
ChainResidueDetails
AASP396metal ligand, proton acceptor, proton donor
AILE397metal ligand
AASP440metal ligand

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PDB entries from 2024-11-06

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