5TVW
Crystal structure of mitochondrial Hsp90 (TRAP1) with ATP in absence of Mg, hemi-hydrolyzed
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005743 | cellular_component | mitochondrial inner membrane |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0006457 | biological_process | protein folding |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| A | 0019901 | molecular_function | protein kinase binding |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0051082 | molecular_function | unfolded protein binding |
| A | 0070013 | cellular_component | intracellular organelle lumen |
| A | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005743 | cellular_component | mitochondrial inner membrane |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0006457 | biological_process | protein folding |
| B | 0016887 | molecular_function | ATP hydrolysis activity |
| B | 0019901 | molecular_function | protein kinase binding |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0051082 | molecular_function | unfolded protein binding |
| B | 0070013 | cellular_component | intracellular organelle lumen |
| B | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | binding site for residue ADP A 801 |
| Chain | Residue |
| A | ASN134 |
| A | GLY214 |
| A | GLN215 |
| A | PHE216 |
| A | GLY217 |
| A | VAL218 |
| A | GLY219 |
| A | PHE220 |
| A | THR266 |
| A | HOH914 |
| A | HOH923 |
| A | ALA138 |
| A | HOH931 |
| A | HOH965 |
| A | HOH966 |
| A | LYS141 |
| A | ASP173 |
| A | MET178 |
| A | ASN186 |
| A | SER193 |
| A | GLY194 |
| A | SER195 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | binding site for residue CO A 802 |
| Chain | Residue |
| A | ASP92 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue CO A 803 |
| Chain | Residue |
| A | ASN204 |
| A | HOH926 |
| A | HOH972 |
| B | GLU592 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | binding site for residue CO B 801 |
| Chain | Residue |
| B | MET505 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | binding site for residue CO B 802 |
| Chain | Residue |
| B | ASP92 |
| site_id | AC6 |
| Number of Residues | 23 |
| Details | binding site for residue ATP B 803 |
| Chain | Residue |
| B | ASN134 |
| B | ALA138 |
| B | LYS141 |
| B | ASP173 |
| B | MET178 |
| B | ASN186 |
| B | SER193 |
| B | GLY194 |
| B | SER195 |
| B | GLY214 |
| B | GLN215 |
| B | PHE216 |
| B | GLY217 |
| B | VAL218 |
| B | GLY219 |
| B | PHE220 |
| B | THR266 |
| B | ARG417 |
| B | HOH902 |
| B | HOH916 |
| B | HOH919 |
| B | HOH933 |
| B | HOH939 |
