4J0B
Structure of mitochondrial Hsp90 (TRAP1) with ADP-BeF3
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 | 0005739 | cellular_component | mitochondrion |
| A | 0005743 | cellular_component | mitochondrial inner membrane |
| 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 | 0046872 | molecular_function | metal ion binding |
| A | 0051082 | molecular_function | unfolded protein binding |
| 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 | 0005739 | cellular_component | mitochondrion |
| B | 0005743 | cellular_component | mitochondrial inner membrane |
| 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 | 0046872 | molecular_function | metal ion binding |
| B | 0051082 | molecular_function | unfolded protein binding |
| B | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CO A 801 |
| Chain | Residue |
| A | ASN95 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CO A 802 |
| Chain | Residue |
| A | LEU202 |
| A | ASN204 |
| site_id | AC3 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE ADP A 803 |
| Chain | Residue |
| A | SER193 |
| A | GLY194 |
| A | SER195 |
| A | GLY214 |
| A | GLN215 |
| A | PHE216 |
| A | GLY217 |
| A | VAL218 |
| A | GLY219 |
| A | PHE220 |
| A | THR266 |
| A | BEF804 |
| A | MG805 |
| A | HOH902 |
| A | HOH905 |
| A | HOH910 |
| A | HOH917 |
| A | HOH923 |
| A | HOH966 |
| A | HOH972 |
| A | ASN134 |
| A | ALA138 |
| A | LYS141 |
| A | ASP173 |
| A | MET178 |
| A | ASN186 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE BEF A 804 |
| Chain | Residue |
| A | GLU130 |
| A | GLY214 |
| A | GLN215 |
| A | PHE216 |
| A | GLY217 |
| A | VAL218 |
| A | GLY219 |
| A | ARG417 |
| A | ADP803 |
| A | MG805 |
| A | HOH917 |
| A | HOH918 |
| A | HOH960 |
| A | HOH970 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 805 |
| Chain | Residue |
| A | ASN134 |
| A | ADP803 |
| A | BEF804 |
| A | HOH917 |
| A | HOH960 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CO B 802 |
| Chain | Residue |
| B | ASP92 |
| site_id | AC7 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE ADP 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 | BEF804 |
| B | MG805 |
| B | HOH903 |
| B | HOH905 |
| B | HOH906 |
| B | HOH907 |
| B | HOH919 |
| B | HOH954 |
| B | HOH975 |
| site_id | AC8 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE BEF B 804 |
| Chain | Residue |
| B | GLU130 |
| B | GLY214 |
| B | GLN215 |
| B | PHE216 |
| B | GLY217 |
| B | VAL218 |
| B | GLY219 |
| B | ARG417 |
| B | ADP803 |
| B | MG805 |
| B | HOH906 |
| B | HOH919 |
| B | HOH933 |
| B | HOH948 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 805 |
| Chain | Residue |
| B | ASN134 |
| B | ADP803 |
| B | BEF804 |
| B | HOH906 |
| B | HOH919 |
