3RUV
Crystal structure of Cpn-rls in complex with ATP analogue from Methanococcus maripaludis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006457 | biological_process | protein folding |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| A | 0032991 | cellular_component | protein-containing complex |
| 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 | 0000166 | molecular_function | nucleotide binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006457 | biological_process | protein folding |
| B | 0016887 | molecular_function | ATP hydrolysis activity |
| B | 0032991 | cellular_component | protein-containing complex |
| 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 | 0000166 | molecular_function | nucleotide binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006457 | biological_process | protein folding |
| C | 0016887 | molecular_function | ATP hydrolysis activity |
| C | 0032991 | cellular_component | protein-containing complex |
| 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 | 0000166 | molecular_function | nucleotide binding |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006457 | biological_process | protein folding |
| D | 0016887 | molecular_function | ATP hydrolysis activity |
| D | 0032991 | cellular_component | protein-containing complex |
| 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 | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 544 |
| Chain | Residue |
| A | ASP91 |
| A | ANP545 |
| A | HOH550 |
| A | HOH669 |
| site_id | AC2 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE ANP A 545 |
| Chain | Residue |
| A | ASP60 |
| A | GLY61 |
| A | ASP91 |
| A | GLY92 |
| A | THR93 |
| A | THR94 |
| A | THR95 |
| A | GLY160 |
| A | LYS161 |
| A | GLY403 |
| A | GLY404 |
| A | LEU444 |
| A | LEU473 |
| A | ASN474 |
| A | VAL475 |
| A | PHE476 |
| A | VAL488 |
| A | GLU490 |
| A | MG544 |
| A | HOH552 |
| A | HOH561 |
| A | HOH567 |
| A | HOH591 |
| A | HOH592 |
| A | HOH599 |
| A | THR38 |
| A | LEU39 |
| A | GLY40 |
| A | PRO41 |
| A | ASN59 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 546 |
| Chain | Residue |
| A | LYS216 |
| A | ARG307 |
| A | ARG308 |
| A | HOH694 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 547 |
| Chain | Residue |
| A | ARG218 |
| A | LYS225 |
| B | LYS319 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 548 |
| Chain | Residue |
| A | ARG66 |
| A | LYS83 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 549 |
| Chain | Residue |
| A | ASP60 |
| A | ASP386 |
| A | HOH560 |
| A | HOH561 |
| A | HOH562 |
| A | HOH563 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 544 |
| Chain | Residue |
| B | ASP91 |
| B | ANP545 |
| B | HOH631 |
| B | HOH676 |
| site_id | AC8 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE ANP B 545 |
| Chain | Residue |
| B | THR38 |
| B | LEU39 |
| B | GLY40 |
| B | PRO41 |
| B | ASN59 |
| B | ASP60 |
| B | GLY61 |
| B | ASP91 |
| B | GLY92 |
| B | THR93 |
| B | THR94 |
| B | THR95 |
| B | GLY160 |
| B | LYS161 |
| B | GLY403 |
| B | GLY404 |
| B | LEU473 |
| B | ASN474 |
| B | PHE476 |
| B | VAL488 |
| B | GLU490 |
| B | MG544 |
| B | HOH552 |
| B | HOH561 |
| B | HOH567 |
| B | HOH589 |
| B | HOH593 |
| B | HOH594 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 546 |
| Chain | Residue |
| B | LYS216 |
| B | ARG307 |
| B | ARG308 |
| B | HOH657 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 547 |
| Chain | Residue |
| B | ARG218 |
| B | LYS225 |
| B | HOH666 |
| C | LYS319 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 548 |
| Chain | Residue |
| B | ARG66 |
| B | LYS83 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 549 |
| Chain | Residue |
| B | ASP60 |
| B | ASP386 |
| B | HOH567 |
| B | HOH568 |
| B | HOH569 |
| B | HOH570 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG C 544 |
| Chain | Residue |
| C | HOH551 |
| C | HOH553 |
| C | ASP91 |
| C | ANP545 |
| site_id | BC5 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE ANP C 545 |
| Chain | Residue |
| C | THR38 |
| C | LEU39 |
| C | GLY40 |
| C | PRO41 |
| C | ASN59 |
| C | ASP60 |
| C | GLY61 |
| C | ASP91 |
| C | GLY92 |
| C | THR93 |
| C | THR94 |
| C | THR95 |
| C | GLY160 |
| C | LYS161 |
| C | ASP386 |
| C | GLY403 |
| C | GLY404 |
| C | LEU473 |
| C | ASN474 |
| C | PHE476 |
| C | VAL488 |
| C | GLU490 |
| C | MG544 |
| C | HOH550 |
| C | HOH554 |
| C | HOH556 |
| C | HOH574 |
| C | HOH595 |
| C | HOH596 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 C 546 |
| Chain | Residue |
| C | LYS216 |
| C | ARG307 |
| C | ARG308 |
| C | HOH689 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 C 547 |
| Chain | Residue |
| C | ARG218 |
| C | LYS225 |
| C | HOH552 |
| C | HOH688 |
| D | LYS319 |
| site_id | BC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 C 548 |
| Chain | Residue |
| C | ARG66 |
| C | LYS83 |
| site_id | BC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG C 549 |
| Chain | Residue |
| C | ASP60 |
| C | GLY90 |
| C | ASP386 |
| C | HOH572 |
| C | HOH573 |
| C | HOH574 |
| C | HOH672 |
| site_id | CC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG D 544 |
| Chain | Residue |
| D | ASP91 |
| D | ANP545 |
| D | HOH638 |
| D | HOH639 |
| site_id | CC2 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE ANP D 545 |
| Chain | Residue |
| D | THR38 |
| D | LEU39 |
| D | GLY40 |
| D | PRO41 |
| D | ASN59 |
| D | ASP60 |
| D | GLY61 |
| D | ASP91 |
| D | GLY92 |
| D | THR93 |
| D | THR94 |
| D | THR95 |
| D | GLY160 |
| D | LYS161 |
| D | ASP386 |
| D | GLY403 |
| D | GLY404 |
| D | LEU473 |
| D | ASN474 |
| D | VAL475 |
| D | PHE476 |
| D | VAL488 |
| D | GLU490 |
| D | MG544 |
| D | HOH550 |
| D | HOH551 |
| D | HOH560 |
| D | HOH577 |
| D | HOH597 |
| D | HOH598 |
| D | HOH638 |
| D | HOH647 |
| site_id | CC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 D 546 |
| Chain | Residue |
| D | LYS216 |
| D | ARG307 |
| D | ARG308 |
| site_id | CC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 D 547 |
| Chain | Residue |
| A | LYS319 |
| D | ARG218 |
| D | LYS225 |
| site_id | CC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 D 548 |
| Chain | Residue |
| D | ARG66 |
| D | LYS83 |
| site_id | CC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG D 549 |
| Chain | Residue |
| D | ASP60 |
| D | ASP386 |
| D | HOH577 |
| D | HOH578 |
| D | HOH579 |
| D | HOH580 |
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 |
