3MAA
Complex of GS-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Adenosine 5-O-(l-Thiophosphate) and Low Ca Concentration
Replaces: 3E8AFunctional Information from GO Data
Chain | GOid | namespace | contents |
A | 0009190 | biological_process | cyclic nucleotide biosynthetic process |
A | 0016849 | molecular_function | phosphorus-oxygen lyase activity |
A | 0035556 | biological_process | intracellular signal transduction |
B | 0009190 | biological_process | cyclic nucleotide biosynthetic process |
B | 0016849 | molecular_function | phosphorus-oxygen lyase activity |
B | 0035556 | biological_process | intracellular signal transduction |
C | 0003924 | molecular_function | GTPase activity |
C | 0005159 | molecular_function | insulin-like growth factor receptor binding |
C | 0005525 | molecular_function | GTP binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0005834 | cellular_component | heterotrimeric G-protein complex |
C | 0005886 | cellular_component | plasma membrane |
C | 0007165 | biological_process | signal transduction |
C | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
C | 0007189 | biological_process | adenylate cyclase-activating G protein-coupled receptor signaling pathway |
C | 0007191 | biological_process | adenylate cyclase-activating dopamine receptor signaling pathway |
C | 0007606 | biological_process | sensory perception of chemical stimulus |
C | 0010856 | molecular_function | adenylate cyclase activator activity |
C | 0019001 | molecular_function | guanyl nucleotide binding |
C | 0031683 | molecular_function | G-protein beta/gamma-subunit complex binding |
C | 0031698 | molecular_function | beta-2 adrenergic receptor binding |
C | 0031748 | molecular_function | D1 dopamine receptor binding |
C | 0031852 | molecular_function | mu-type opioid receptor binding |
C | 0035255 | molecular_function | ionotropic glutamate receptor binding |
C | 0046872 | molecular_function | metal ion binding |
C | 0051430 | molecular_function | corticotropin-releasing hormone receptor 1 binding |
C | 0071880 | biological_process | adenylate cyclase-activating adrenergic receptor signaling pathway |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE FKP A 101 |
Chain | Residue |
A | PHE394 |
B | PHE895 |
B | LYS896 |
B | TYR899 |
B | ILE940 |
B | GLY941 |
B | SER942 |
A | TYR443 |
A | VAL506 |
A | TRP507 |
A | SER508 |
A | VAL511 |
A | THR512 |
B | TAT1 |
B | HOH17 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CA A 581 |
Chain | Residue |
A | ASP396 |
A | ASP440 |
B | TAT1 |
site_id | AC3 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE TAT B 1 |
Chain | Residue |
A | FKP101 |
A | THR401 |
A | LEU438 |
A | ASP440 |
A | CA581 |
B | LYS938 |
B | MET945 |
B | ASP1018 |
B | ILE1019 |
B | VAL1024 |
B | ASN1025 |
B | SER1028 |
B | ARG1029 |
B | HOH1082 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG C 396 |
Chain | Residue |
C | SER54 |
C | THR204 |
C | GSP395 |
site_id | AC5 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE GSP C 395 |
Chain | Residue |
C | ALA48 |
C | GLU50 |
C | SER51 |
C | GLY52 |
C | LYS53 |
C | SER54 |
C | THR55 |
C | ASP173 |
C | LEU198 |
C | ARG199 |
C | ARG201 |
C | THR204 |
C | GLY226 |
C | ASN292 |
C | LYS293 |
C | ASP295 |
C | LEU296 |
C | CYS365 |
C | ALA366 |
C | VAL367 |
C | MG396 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL C 397 |
Chain | Residue |
C | ALA48 |
C | ALA249 |
C | HOH398 |
Functional Information from PROSITE/UniProt
site_id | PS00452 |
Number of Residues | 24 |
Details | GUANYLATE_CYCLASE_1 Guanylate cyclase signature. GVL.GlrkwqFdVWSNDVTlanhmE |
Chain | Residue | Details |
A | GLY495-GLU518 | |
B | GLY1008-ASP1031 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 5 |
Details | BINDING: 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 |
Chain | Residue | Details |
C | GLY47 | |
C | LEU197 | |
C | ASP223 | |
C | ASN292 | |
C | ALA366 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: 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 |
Chain | Residue | Details |
C | SER54 | |
C | THR204 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P63092 |
Chain | Residue | Details |
C | SER352 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | LIPID: N-palmitoyl glycine => ECO:0000269|PubMed:12574119 |
Chain | Residue | Details |
C | GLY2 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | LIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:12574119 |
Chain | Residue | Details |
C | CYS3 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P63092 |
Chain | Residue | Details |
C | LYS300 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 2 |
Details | M-CSA 58 |
Chain | Residue | Details |
B | ARG1029 | electrostatic stabiliser |
B | LYS1065 | electrostatic stabiliser |
A | ASP440 | metal ligand |