4IPE
Crystal structure of mitochondrial Hsp90 (TRAP1) with AMPPNP
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 | 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 |