1AZT
GS-ALPHA COMPLEXED WITH GTP-GAMMA-S
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003924 | molecular_function | GTPase activity |
| A | 0005159 | molecular_function | insulin-like growth factor receptor binding |
| A | 0005525 | molecular_function | GTP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005834 | cellular_component | heterotrimeric G-protein complex |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0007165 | biological_process | signal transduction |
| A | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
| A | 0007189 | biological_process | adenylate cyclase-activating G protein-coupled receptor signaling pathway |
| A | 0007191 | biological_process | adenylate cyclase-activating dopamine receptor signaling pathway |
| A | 0007606 | biological_process | sensory perception of chemical stimulus |
| A | 0010856 | molecular_function | adenylate cyclase activator activity |
| A | 0016020 | cellular_component | membrane |
| A | 0019001 | molecular_function | guanyl nucleotide binding |
| A | 0031683 | molecular_function | G-protein beta/gamma-subunit complex binding |
| A | 0031698 | molecular_function | beta-2 adrenergic receptor binding |
| A | 0031748 | molecular_function | D1 dopamine receptor binding |
| A | 0031852 | molecular_function | mu-type opioid receptor binding |
| A | 0035255 | molecular_function | ionotropic glutamate receptor binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051430 | molecular_function | corticotropin-releasing hormone receptor 1 binding |
| A | 0051716 | biological_process | cellular response to stimulus |
| A | 0071880 | biological_process | adenylate cyclase-activating adrenergic receptor signaling pathway |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003924 | molecular_function | GTPase activity |
| B | 0005159 | molecular_function | insulin-like growth factor receptor binding |
| B | 0005525 | molecular_function | GTP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005834 | cellular_component | heterotrimeric G-protein complex |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0007165 | biological_process | signal transduction |
| B | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
| B | 0007189 | biological_process | adenylate cyclase-activating G protein-coupled receptor signaling pathway |
| B | 0007191 | biological_process | adenylate cyclase-activating dopamine receptor signaling pathway |
| B | 0007606 | biological_process | sensory perception of chemical stimulus |
| B | 0010856 | molecular_function | adenylate cyclase activator activity |
| B | 0016020 | cellular_component | membrane |
| B | 0019001 | molecular_function | guanyl nucleotide binding |
| B | 0031683 | molecular_function | G-protein beta/gamma-subunit complex binding |
| B | 0031698 | molecular_function | beta-2 adrenergic receptor binding |
| B | 0031748 | molecular_function | D1 dopamine receptor binding |
| B | 0031852 | molecular_function | mu-type opioid receptor binding |
| B | 0035255 | molecular_function | ionotropic glutamate receptor binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051430 | molecular_function | corticotropin-releasing hormone receptor 1 binding |
| B | 0051716 | biological_process | cellular response to stimulus |
| B | 0071880 | biological_process | adenylate cyclase-activating adrenergic receptor signaling pathway |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 403 |
| Chain | Residue |
| A | SER54 |
| A | THR204 |
| A | ASP223 |
| A | GSP413 |
| A | HOH415 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 404 |
| Chain | Residue |
| B | ASP378 |
| A | ASP378 |
| A | HOH439 |
| B | HIS362 |
| B | ARG374 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 A 405 |
| Chain | Residue |
| A | TYR37 |
| A | ARG42 |
| A | GLU209 |
| A | HIS220 |
| A | PHE222 |
| B | ASP129 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PO4 A 406 |
| Chain | Residue |
| A | ARG61 |
| A | PHE208 |
| A | ASP223 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 B 403 |
| Chain | Residue |
| B | THR325 |
| B | PRO326 |
| B | GLU327 |
| B | LYS338 |
| B | TYR339 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 B 404 |
| Chain | Residue |
| A | ASP381 |
| A | ARG385 |
| B | ASP368 |
| B | ASN371 |
| B | ARG374 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PO4 A 407 |
| Chain | Residue |
| A | ARG199 |
| A | ASP295 |
| A | GLU299 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 B 405 |
| Chain | Residue |
| A | GLU370 |
| A | ARG373 |
| A | ARG374 |
| A | ASN377 |
| B | ASN377 |
| B | ARG380 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 408 |
| Chain | Residue |
| A | HIS64 |
| A | ARG373 |
| A | ASN377 |
| A | ARG380 |
| A | HOH440 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 406 |
| Chain | Residue |
| B | SER54 |
| B | THR204 |
| B | ASP223 |
| B | VAL224 |
| B | GSP411 |
| B | HOH413 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 409 |
| Chain | Residue |
| A | HIS362 |
| A | ARG374 |
| A | ASP378 |
| A | HOH414 |
| B | ASP378 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 B 407 |
| Chain | Residue |
| A | PHE126 |
| A | ASP129 |
| B | TYR37 |
| B | ARG42 |
| B | GLU209 |
| B | HIS220 |
| B | PHE222 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PO4 B 408 |
| Chain | Residue |
| B | ARG61 |
| B | PHE208 |
| B | ASP223 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 A 410 |
| Chain | Residue |
| A | THR325 |
| A | GLU327 |
| A | LYS338 |
| A | PHE363 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 A 411 |
| Chain | Residue |
| A | ASP368 |
| A | GLU370 |
| A | ASN371 |
| A | ARG374 |
| B | ASP381 |
| B | ARG385 |
| site_id | BC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PO4 B 409 |
| Chain | Residue |
| B | ARG199 |
| B | ASP295 |
| B | GLU299 |
| site_id | BC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 A 412 |
| Chain | Residue |
| A | ASN377 |
| A | ARG380 |
| A | HOH440 |
| B | ARG373 |
| B | ARG374 |
| B | ASN377 |
| site_id | BC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 B 410 |
| Chain | Residue |
| A | HOH437 |
| B | HIS64 |
| B | ARG373 |
| B | ASN377 |
| B | HOH435 |
| site_id | CC1 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE GSP A 413 |
| Chain | Residue |
| A | THR204 |
| A | GLY226 |
| A | ASN292 |
| A | LYS293 |
| A | ASP295 |
| A | LEU296 |
| A | CYS365 |
| A | ALA366 |
| A | VAL367 |
| A | MG403 |
| A | HOH415 |
| A | HOH420 |
| A | HOH435 |
| A | HOH438 |
| A | ALA48 |
| A | GLY49 |
| A | GLU50 |
| A | SER51 |
| A | GLY52 |
| A | LYS53 |
| A | SER54 |
| A | THR55 |
| A | ASP173 |
| A | LEU198 |
| A | ARG199 |
| site_id | CC2 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE GSP B 411 |
| Chain | Residue |
| B | ALA48 |
| B | GLY49 |
| B | GLU50 |
| B | SER51 |
| B | GLY52 |
| B | LYS53 |
| B | SER54 |
| B | THR55 |
| B | ASP173 |
| B | LEU198 |
| B | ARG199 |
| B | LEU203 |
| B | THR204 |
| B | GLY226 |
| B | ASN292 |
| B | LYS293 |
| B | ASP295 |
| B | CYS365 |
| B | ALA366 |
| B | VAL367 |
| B | MG406 |
| B | HOH413 |
| B | HOH433 |
| B | HOH438 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| 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 |
| A | GLY47 | |
| B | ALA366 | |
| A | LEU197 | |
| A | ASP223 | |
| A | ASN292 | |
| A | ALA366 | |
| B | GLY47 | |
| B | LEU197 | |
| B | ASP223 | |
| B | ASN292 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| 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 |
| A | SER54 | |
| A | THR204 | |
| B | SER54 | |
| B | THR204 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P63092 |
| Chain | Residue | Details |
| A | SER352 | |
| B | SER352 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | LIPID: N-palmitoyl glycine => ECO:0000269|PubMed:12574119 |
| Chain | Residue | Details |
| A | GLY2 | |
| B | GLY2 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | LIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:12574119 |
| Chain | Residue | Details |
| A | CYS3 | |
| B | CYS3 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P63092 |
| Chain | Residue | Details |
| A | LYS300 | |
| B | LYS300 |
