1AZT
GS-ALPHA COMPLEXED WITH GTP-GAMMA-S
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 0016787 | molecular_function | hydrolase activity |
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 | 0071880 | biological_process | adenylate cyclase-activating adrenergic receptor signaling pathway |
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 | 0016787 | molecular_function | hydrolase activity |
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 | 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 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1ksj |
Chain | Residue | Details |
A | THR204 | |
A | ARG201 | |
A | GLU50 | |
A | GLN227 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1ksj |
Chain | Residue | Details |
B | THR204 | |
B | ARG201 | |
B | GLU50 | |
B | GLN227 |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ksj |
Chain | Residue | Details |
A | GLN227 |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ksj |
Chain | Residue | Details |
B | GLN227 |