3KFK
Crystal structures of a group II chaperonin from Methanococcus maripaludis
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005524 | molecular_function | ATP binding |
A | 0006457 | biological_process | protein folding |
A | 0016887 | molecular_function | ATP hydrolysis activity |
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 | 0005524 | molecular_function | ATP binding |
B | 0006457 | biological_process | protein folding |
B | 0016887 | molecular_function | ATP hydrolysis activity |
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 |
C | 0005524 | molecular_function | ATP binding |
C | 0006457 | biological_process | protein folding |
C | 0016887 | molecular_function | ATP hydrolysis activity |
C | 0042802 | molecular_function | identical protein binding |
C | 0046872 | molecular_function | metal ion binding |
C | 0051082 | molecular_function | unfolded protein binding |
C | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
D | 0005524 | molecular_function | ATP binding |
D | 0006457 | biological_process | protein folding |
D | 0016887 | molecular_function | ATP hydrolysis activity |
D | 0042802 | molecular_function | identical protein binding |
D | 0046872 | molecular_function | metal ion binding |
D | 0051082 | molecular_function | unfolded protein binding |
D | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE AGS A 544 |
Chain | Residue |
A | THR38 |
A | THR95 |
A | GLY403 |
A | GLY404 |
A | LEU473 |
A | ASN474 |
A | PHE476 |
A | GLU490 |
A | LEU39 |
A | GLY40 |
A | PRO41 |
A | ASP60 |
A | GLY61 |
A | ASP91 |
A | THR93 |
A | THR94 |
site_id | AC2 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE AGS B 544 |
Chain | Residue |
B | THR38 |
B | LEU39 |
B | GLY40 |
B | PRO41 |
B | ASP60 |
B | GLY61 |
B | ASP91 |
B | GLY92 |
B | THR93 |
B | THR94 |
B | THR95 |
B | GLY403 |
B | GLY404 |
B | LEU473 |
B | GLU490 |
site_id | AC3 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE AGS C 544 |
Chain | Residue |
C | THR38 |
C | LEU39 |
C | GLY40 |
C | PRO41 |
C | ASP60 |
C | GLY61 |
C | ASP91 |
C | GLY92 |
C | THR93 |
C | THR94 |
C | THR95 |
C | GLY403 |
C | GLY404 |
C | LEU473 |
C | GLU490 |
site_id | AC4 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE AGS D 544 |
Chain | Residue |
D | GLY40 |
D | ASP60 |
D | ASP91 |
D | GLY92 |
D | THR93 |
D | THR94 |
D | THR95 |
D | GLY403 |
D | GLY404 |
D | LEU473 |
D | ASN474 |
D | VAL488 |
D | GLU490 |
Functional Information from PROSITE/UniProt
site_id | PS00750 |
Number of Residues | 13 |
Details | TCP1_1 Chaperonins TCP-1 signature 1. RStLGPkGmdKML |
Chain | Residue | Details |
A | ARG36-LEU48 |
site_id | PS00751 |
Number of Residues | 17 |
Details | TCP1_2 Chaperonins TCP-1 signature 2. VTNDGVTILreMsVeHP |
Chain | Residue | Details |
A | VAL57-PRO73 |
site_id | PS00995 |
Number of Residues | 9 |
Details | TCP1_3 Chaperonins TCP-1 signature 3. QEkeVGDGT |
Chain | Residue | Details |
A | GLN85-THR93 |