4XTR
Structure of Get3 bound to the transmembrane domain of Pep12
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000750 | biological_process | pheromone-dependent signal transduction involved in conjugation with cellular fusion |
| A | 0005085 | molecular_function | guanyl-nucleotide exchange factor activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005789 | cellular_component | endoplasmic reticulum membrane |
| A | 0005794 | cellular_component | Golgi apparatus |
| A | 0005829 | cellular_component | cytosol |
| A | 0006457 | biological_process | protein folding |
| A | 0006620 | biological_process | post-translational protein targeting to endoplasmic reticulum membrane |
| A | 0006890 | biological_process | retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0009408 | biological_process | response to heat |
| A | 0010038 | biological_process | response to metal ion |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| A | 0034599 | biological_process | cellular response to oxidative stress |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0043529 | cellular_component | GET complex |
| A | 0044183 | molecular_function | protein folding chaperone |
| A | 0045048 | biological_process | protein insertion into ER membrane |
| A | 0051082 | molecular_function | unfolded protein binding |
| A | 0071816 | biological_process | tail-anchored membrane protein insertion into ER membrane |
| B | 0000750 | biological_process | pheromone-dependent signal transduction involved in conjugation with cellular fusion |
| B | 0005085 | molecular_function | guanyl-nucleotide exchange factor activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005783 | cellular_component | endoplasmic reticulum |
| B | 0005789 | cellular_component | endoplasmic reticulum membrane |
| B | 0005794 | cellular_component | Golgi apparatus |
| B | 0005829 | cellular_component | cytosol |
| B | 0006457 | biological_process | protein folding |
| B | 0006620 | biological_process | post-translational protein targeting to endoplasmic reticulum membrane |
| B | 0006890 | biological_process | retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0009408 | biological_process | response to heat |
| B | 0010038 | biological_process | response to metal ion |
| B | 0016887 | molecular_function | ATP hydrolysis activity |
| B | 0034599 | biological_process | cellular response to oxidative stress |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0043529 | cellular_component | GET complex |
| B | 0044183 | molecular_function | protein folding chaperone |
| B | 0045048 | biological_process | protein insertion into ER membrane |
| B | 0051082 | molecular_function | unfolded protein binding |
| B | 0071816 | biological_process | tail-anchored membrane protein insertion into ER membrane |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | binding site for residue ADP A 401 |
| Chain | Residue |
| A | GLY28 |
| A | ILE321 |
| A | PHE330 |
| A | MG402 |
| A | ATP404 |
| A | HOH506 |
| A | HOH509 |
| A | HOH592 |
| B | LYS26 |
| B | GLU245 |
| B | LEU247 |
| A | VAL29 |
| A | GLY30 |
| A | LYS31 |
| A | THR32 |
| A | THR33 |
| A | ASN272 |
| A | PRO315 |
| A | CYS317 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 402 |
| Chain | Residue |
| A | THR32 |
| A | ADP401 |
| A | ATP404 |
| A | HOH505 |
| A | HOH506 |
| A | HOH559 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 403 |
| Chain | Residue |
| A | CYS285 |
| A | CYS288 |
| B | CYS285 |
| B | CYS288 |
| site_id | AC4 |
| Number of Residues | 25 |
| Details | binding site for residue ATP A 404 |
| Chain | Residue |
| A | GLY27 |
| A | GLY28 |
| A | VAL29 |
| A | GLY30 |
| A | LYS31 |
| A | THR32 |
| A | THR33 |
| A | ASN57 |
| A | PRO169 |
| A | ASN272 |
| A | PRO315 |
| A | LEU316 |
| A | CYS317 |
| A | ILE321 |
| A | PHE330 |
| A | ADP401 |
| A | MG402 |
| A | HOH506 |
| A | HOH509 |
| A | HOH592 |
| A | HOH595 |
| B | LYS26 |
| B | GLY27 |
| B | GLU245 |
| B | LEU247 |
| site_id | AC5 |
| Number of Residues | 21 |
| Details | binding site for residue ADP B 401 |
| Chain | Residue |
| A | LYS26 |
| A | GLU245 |
| A | PHE246 |
| A | LEU247 |
| B | GLY28 |
| B | VAL29 |
| B | GLY30 |
| B | LYS31 |
| B | THR32 |
| B | THR33 |
| B | ASN272 |
| B | PRO315 |
| B | LEU316 |
| B | CYS317 |
| B | ILE321 |
| B | PHE330 |
| B | MG402 |
| B | ATP403 |
| B | HOH545 |
| B | HOH557 |
| B | HOH611 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 402 |
| Chain | Residue |
| B | THR32 |
| B | ADP401 |
| B | ATP403 |
| B | HOH528 |
| B | HOH571 |
| B | HOH611 |
| site_id | AC7 |
| Number of Residues | 27 |
| Details | binding site for residue ATP B 403 |
| Chain | Residue |
| B | PHE330 |
| B | ADP401 |
| B | MG402 |
| B | HOH528 |
| B | HOH545 |
| B | HOH557 |
| B | HOH571 |
| B | HOH611 |
| B | HOH619 |
| A | LYS26 |
| A | GLY27 |
| A | GLU245 |
| A | PHE246 |
| A | LEU247 |
| B | GLY27 |
| B | GLY28 |
| B | VAL29 |
| B | GLY30 |
| B | LYS31 |
| B | THR32 |
| B | THR33 |
| B | ASN57 |
| B | ASN272 |
| B | PRO315 |
| B | LEU316 |
| B | CYS317 |
| B | ILE321 |
Functional Information from PROSITE/UniProt
| site_id | PS00290 |
| Number of Residues | 7 |
| Details | IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YICNVNH |
| Chain | Residue | Details |
| C | TYR203-HIS209 | |
| D | TYR195-HIS201 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 32 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03112","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19675567","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
