6TMU
Crystal structure of the chaperonin gp146 from the bacteriophage EL 2 (Pseudomonas aeruginosa) in presence of ATP-BeFx, crystal form II
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 | 2 |
Details | binding site for residue MG A 601 |
Chain | Residue |
A | ASP86 |
A | ATP603 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue K A 602 |
Chain | Residue |
A | THR30 |
A | LYS50 |
A | ATP603 |
site_id | AC3 |
Number of Residues | 22 |
Details | binding site for residue ATP A 603 |
Chain | Residue |
A | ASP86 |
A | GLY87 |
A | THR89 |
A | THR90 |
A | THR145 |
A | GLN149 |
A | GLY428 |
A | GLY429 |
A | GLY430 |
A | GLN474 |
A | LEU478 |
A | MET504 |
A | ASN505 |
A | LEU506 |
A | ILE519 |
A | ASP521 |
A | MG601 |
A | K602 |
A | THR30 |
A | MET31 |
A | GLY32 |
A | GLY52 |
site_id | AC4 |
Number of Residues | 11 |
Details | binding site for residue ADP B 600 |
Chain | Residue |
B | THR30 |
B | ASP86 |
B | GLY87 |
B | THR88 |
B | THR89 |
B | THR90 |
B | MET504 |
B | ASN505 |
B | LEU506 |
B | ILE519 |
B | ASP521 |
site_id | AC5 |
Number of Residues | 2 |
Details | binding site for residue MG C 601 |
Chain | Residue |
C | ASP86 |
C | ATP603 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue K C 602 |
Chain | Residue |
C | THR30 |
C | LYS50 |
C | ATP603 |
site_id | AC7 |
Number of Residues | 20 |
Details | binding site for residue ATP C 603 |
Chain | Residue |
C | MET31 |
C | GLY32 |
C | GLY52 |
C | ASP86 |
C | GLY87 |
C | THR88 |
C | THR89 |
C | THR90 |
C | THR145 |
C | GLY428 |
C | GLY429 |
C | GLY430 |
C | GLN474 |
C | MET504 |
C | ASN505 |
C | LEU506 |
C | ILE519 |
C | ASP521 |
C | MG601 |
C | K602 |
site_id | AC8 |
Number of Residues | 12 |
Details | binding site for residue ADP D 600 |
Chain | Residue |
D | MET31 |
D | ASP86 |
D | GLY87 |
D | THR88 |
D | THR89 |
D | THR90 |
D | LEU478 |
D | MET504 |
D | ASN505 |
D | LEU506 |
D | ILE519 |
D | ASP521 |
site_id | AC9 |
Number of Residues | 2 |
Details | binding site for residue MG E 601 |
Chain | Residue |
E | ASP86 |
E | ATP603 |
site_id | AD1 |
Number of Residues | 3 |
Details | binding site for residue K E 602 |
Chain | Residue |
E | THR30 |
E | LYS50 |
E | ATP603 |
site_id | AD2 |
Number of Residues | 22 |
Details | binding site for residue ATP E 603 |
Chain | Residue |
E | ASP521 |
E | MG601 |
E | K602 |
E | MET31 |
E | GLY32 |
E | GLY52 |
E | ASP86 |
E | GLY87 |
E | THR88 |
E | THR89 |
E | THR90 |
E | THR145 |
E | GLN149 |
E | GLY428 |
E | GLY429 |
E | GLY430 |
E | GLN474 |
E | LEU478 |
E | MET504 |
E | ASN505 |
E | LEU506 |
E | ILE519 |
site_id | AD3 |
Number of Residues | 11 |
Details | binding site for residue ADP F 600 |
Chain | Residue |
F | GLY32 |
F | ASP86 |
F | GLY87 |
F | THR88 |
F | THR89 |
F | THR90 |
F | MET504 |
F | ASN505 |
F | LEU506 |
F | ILE519 |
F | ASP521 |
site_id | AD4 |
Number of Residues | 2 |
Details | binding site for residue MG G 601 |
Chain | Residue |
G | ASP86 |
G | ATP603 |
site_id | AD5 |
Number of Residues | 3 |
Details | binding site for residue K G 602 |
Chain | Residue |
G | THR30 |
G | LYS50 |
G | ATP603 |
site_id | AD6 |
Number of Residues | 20 |
Details | binding site for residue ATP G 603 |
Chain | Residue |
G | MET31 |
G | GLY32 |
G | GLY52 |
G | ASP86 |
G | GLY87 |
G | THR88 |
G | THR89 |
G | THR90 |
G | THR145 |
G | GLY428 |
G | GLY429 |
G | GLY430 |
G | GLN474 |
G | MET504 |
G | ASN505 |
G | LEU506 |
G | ILE519 |
G | ASP521 |
G | MG601 |
G | K602 |