6TMT
Crystal structure of the chaperonin gp146 from the bacteriophage EL 2 (Pseudomonas aeruginosa) in presence of ATP-BeFx, crystal form I
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0042026 | biological_process | protein refolding |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0042026 | biological_process | protein refolding |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0042026 | biological_process | protein refolding |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0005524 | molecular_function | ATP binding |
| D | 0042026 | biological_process | protein refolding |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0005524 | molecular_function | ATP binding |
| E | 0042026 | biological_process | protein refolding |
| E | 0042802 | molecular_function | identical protein binding |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0005524 | molecular_function | ATP binding |
| F | 0042026 | biological_process | protein refolding |
| F | 0042802 | molecular_function | identical protein binding |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| G | 0000166 | molecular_function | nucleotide binding |
| G | 0005524 | molecular_function | ATP binding |
| G | 0042026 | biological_process | protein refolding |
| G | 0042802 | molecular_function | identical protein binding |
| G | 0046872 | molecular_function | metal ion binding |
| G | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 601 |
| Chain | Residue |
| A | ASP51 |
| A | ASP86 |
| A | ASP412 |
| A | ATP602 |
| site_id | AC2 |
| Number of Residues | 21 |
| Details | binding site for residue ATP A 602 |
| Chain | Residue |
| A | ASP86 |
| A | GLY87 |
| A | THR88 |
| A | THR89 |
| A | THR90 |
| A | THR145 |
| A | GLN149 |
| A | GLY428 |
| A | GLY429 |
| A | GLN474 |
| A | MET504 |
| A | ASN505 |
| A | LEU506 |
| A | ILE519 |
| A | ASP521 |
| A | MG601 |
| A | MET31 |
| A | GLY32 |
| A | GLY52 |
| A | VAL53 |
| A | ASP81 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue MG B 601 |
| Chain | Residue |
| B | ASP51 |
| B | ASP86 |
| B | SER146 |
| B | ATP602 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | binding site for residue ATP B 602 |
| Chain | Residue |
| B | MET31 |
| B | GLY32 |
| B | PRO33 |
| B | ASP51 |
| B | GLY52 |
| B | VAL53 |
| B | ASP81 |
| B | ASP86 |
| B | GLY87 |
| B | THR88 |
| B | THR89 |
| B | THR90 |
| B | THR145 |
| B | GLY428 |
| B | GLY429 |
| B | GLN474 |
| B | MET504 |
| B | ASN505 |
| B | LEU506 |
| B | ILE519 |
| B | ASP521 |
| B | MG601 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue MG C 601 |
| Chain | Residue |
| C | ASP51 |
| C | ASP86 |
| C | ATP602 |
| site_id | AC6 |
| Number of Residues | 21 |
| Details | binding site for residue ATP C 602 |
| Chain | Residue |
| C | MET31 |
| C | GLY32 |
| C | PRO33 |
| C | GLY52 |
| C | VAL53 |
| C | ASP81 |
| C | ASP86 |
| C | GLY87 |
| C | THR88 |
| C | THR89 |
| C | THR90 |
| C | THR145 |
| C | GLY428 |
| C | GLY429 |
| C | GLN474 |
| C | MET504 |
| C | ASN505 |
| C | LEU506 |
| C | ILE519 |
| C | ASP521 |
| C | MG601 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue MG D 601 |
| Chain | Residue |
| D | ASP51 |
| D | ASP86 |
| D | ASP412 |
| D | ATP602 |
| site_id | AC8 |
| Number of Residues | 21 |
| Details | binding site for residue ATP D 602 |
| Chain | Residue |
| D | MG601 |
| D | GLY32 |
| D | PRO33 |
| D | GLY52 |
| D | VAL53 |
| D | ASP81 |
| D | ASP86 |
| D | GLY87 |
| D | THR88 |
| D | THR89 |
| D | THR90 |
| D | THR145 |
| D | GLN149 |
| D | GLY428 |
| D | GLY429 |
| D | GLN474 |
| D | MET504 |
| D | ASN505 |
| D | LEU506 |
| D | ILE519 |
| D | ASP521 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue MG E 601 |
| Chain | Residue |
| E | ASP51 |
| E | ASP86 |
| E | ATP602 |
| site_id | AD1 |
| Number of Residues | 22 |
| Details | binding site for residue ATP E 602 |
| Chain | Residue |
| E | MET31 |
| E | GLY32 |
| E | ASP51 |
| E | GLY52 |
| E | VAL53 |
| E | ASP81 |
| E | ASP86 |
| E | GLY87 |
| E | THR88 |
| E | THR89 |
| E | THR90 |
| E | THR145 |
| E | GLN149 |
| E | GLY428 |
| E | GLY429 |
| E | GLN474 |
| E | MET504 |
| E | ASN505 |
| E | LEU506 |
| E | ILE519 |
| E | ASP521 |
| E | MG601 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue MG F 601 |
| Chain | Residue |
| F | ASP51 |
| F | ASP86 |
| F | ASP412 |
| F | ATP602 |
| site_id | AD3 |
| Number of Residues | 20 |
| Details | binding site for residue ATP F 602 |
| Chain | Residue |
| F | GLY32 |
| F | PRO33 |
| F | GLY52 |
| F | VAL53 |
| F | ASP81 |
| F | ASP86 |
| F | GLY87 |
| F | THR88 |
| F | THR89 |
| F | THR90 |
| F | THR145 |
| F | GLN149 |
| F | GLY428 |
| F | GLY429 |
| F | GLN474 |
| F | MET504 |
| F | ASN505 |
| F | LEU506 |
| F | ASP521 |
| F | MG601 |
| site_id | AD4 |
| Number of Residues | 22 |
| Details | binding site for residue ATP G 600 |
| Chain | Residue |
| G | MET31 |
| G | GLY32 |
| G | PRO33 |
| G | GLY52 |
| G | VAL53 |
| G | ASP81 |
| G | ASP86 |
| G | GLY87 |
| G | THR88 |
| G | THR89 |
| G | THR90 |
| G | THR145 |
| G | GLN149 |
| G | GLY428 |
| G | GLY429 |
| G | GLN474 |
| G | MET504 |
| G | ASN505 |
| G | LEU506 |
| G | ILE519 |
| G | ASP521 |
| G | MG601 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue MG G 601 |
| Chain | Residue |
| G | ASP51 |
| G | ASP86 |
| G | ASP412 |
| G | ATP600 |
