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
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 | 0016020 | cellular_component | membrane |
C | 0016787 | molecular_function | hydrolase 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 | 4 |
Details | BINDING SITE FOR RESIDUE MN C 396 |
Chain | Residue |
C | SER54 |
C | THR204 |
C | ASP223 |
C | GSP395 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL C 397 |
Chain | Residue |
C | ALA48 |
C | VAL248 |
C | ALA249 |
C | ARG265 |
C | ALA269 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE MN A 581 |
Chain | Residue |
A | ONA100 |
A | ASP440 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MN A 582 |
Chain | Residue |
A | ONA100 |
A | ASP396 |
A | ILE397 |
A | ASP440 |
site_id | AC5 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE GSP C 395 |
Chain | Residue |
C | GLU50 |
C | SER51 |
C | GLY52 |
C | LYS53 |
C | SER54 |
C | THR55 |
C | ASP173 |
C | LEU198 |
C | ARG199 |
C | ARG201 |
C | VAL202 |
C | LEU203 |
C | THR204 |
C | VAL224 |
C | GLY226 |
C | ASN292 |
C | LYS293 |
C | ASP295 |
C | LEU296 |
C | CYS365 |
C | ALA366 |
C | VAL367 |
C | MN396 |
site_id | AC6 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE FKP A 1 |
Chain | Residue |
A | PHE394 |
A | CYS441 |
A | VAL506 |
A | TRP507 |
A | SER508 |
A | VAL511 |
A | THR512 |
A | GLU518 |
B | LYS896 |
B | ILE940 |
B | SER942 |
B | THR943 |
site_id | AC7 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE ONA A 100 |
Chain | Residue |
A | ASP396 |
A | ILE397 |
A | GLY399 |
A | PHE400 |
A | THR401 |
A | ALA404 |
A | GLY439 |
A | ASP440 |
A | ARG484 |
A | MN581 |
A | MN582 |
B | ASN1022 |
B | ASN1025 |
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 | 3 |
Details | BINDING: BINDING => ECO:0000305|PubMed:10427002 |
Chain | Residue | Details |
A | ASP396 | |
A | ILE397 | |
A | ASP440 | |
C | ASN292 | |
C | ALA366 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000305|PubMed:10427002, ECO:0000305|PubMed:11087399, ECO:0000305|PubMed:16766715, ECO:0000305|PubMed:19243146 |
Chain | Residue | Details |
A | LEU438 | |
A | ARG484 |
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 | 3 |
Details | M-CSA 58 |
Chain | Residue | Details |
A | ASP396 | metal ligand, proton acceptor, proton donor |
A | ILE397 | metal ligand |
A | ASP440 | metal ligand |