3RUV
Crystal structure of Cpn-rls in complex with ATP analogue from Methanococcus maripaludis
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005524 | molecular_function | ATP binding |
A | 0005832 | cellular_component | chaperonin-containing T-complex |
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 | 0005832 | cellular_component | chaperonin-containing T-complex |
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 | 0005832 | cellular_component | chaperonin-containing T-complex |
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 | 0005832 | cellular_component | chaperonin-containing T-complex |
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 | 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 |