4IPE
Crystal structure of mitochondrial Hsp90 (TRAP1) with AMPPNP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| 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 | 0046872 | molecular_function | metal ion 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 | 0000166 | molecular_function | nucleotide binding |
| 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 | 0046872 | molecular_function | metal ion 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 | 30 |
| Details | BINDING SITE FOR RESIDUE ANP A 801 |
| Chain | Residue |
| A | GLU130 |
| A | GLY214 |
| A | GLN215 |
| A | PHE216 |
| A | GLY217 |
| A | VAL218 |
| A | GLY219 |
| A | PHE220 |
| A | THR266 |
| A | ARG417 |
| A | MG802 |
| A | ASN134 |
| A | HOH902 |
| A | HOH905 |
| A | HOH907 |
| A | HOH910 |
| A | HOH911 |
| A | HOH912 |
| A | HOH935 |
| A | HOH948 |
| A | HOH956 |
| A | HOH958 |
| A | ALA138 |
| A | HOH1006 |
| A | ASP173 |
| A | MET178 |
| A | ASN186 |
| A | SER193 |
| A | GLY194 |
| A | SER195 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 802 |
| Chain | Residue |
| A | ASN134 |
| A | ANP801 |
| A | HOH956 |
| A | HOH958 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CO A 803 |
| Chain | Residue |
| A | ASP92 |
| A | ASN95 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CO A 804 |
| Chain | Residue |
| A | LEU202 |
| A | ASN204 |
| A | HOH990 |
| site_id | AC5 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE ANP B 802 |
| Chain | Residue |
| B | GLU130 |
| B | ASN134 |
| B | ALA138 |
| B | ASP173 |
| B | MET178 |
| B | ASN186 |
| B | LEU187 |
| 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 | MG803 |
| B | HOH901 |
| B | HOH905 |
| B | HOH908 |
| B | HOH933 |
| B | HOH968 |
| B | HOH1015 |
| B | HOH1027 |
| B | HOH1029 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 803 |
| Chain | Residue |
| B | ASN134 |
| B | ANP802 |
| B | HOH968 |
| B | HOH1027 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CO B 804 |
| Chain | Residue |
| B | HOH1007 |
