4I4L
Crystal Structure of Nucleotide-Bound W-W-W ClpX Hexamer
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 | 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 | 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 | 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 | 0051082 | molecular_function | unfolded protein binding |
| D | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| E | 0005524 | molecular_function | ATP binding |
| E | 0006457 | biological_process | protein folding |
| E | 0016887 | molecular_function | ATP hydrolysis activity |
| E | 0051082 | molecular_function | unfolded protein binding |
| E | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| F | 0005524 | molecular_function | ATP binding |
| F | 0006457 | biological_process | protein folding |
| F | 0016887 | molecular_function | ATP hydrolysis activity |
| F | 0051082 | molecular_function | unfolded protein binding |
| F | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ADP A 600 |
| Chain | Residue |
| A | TYR77 |
| A | LEU127 |
| A | ILE325 |
| A | ALA369 |
| A | VAL78 |
| A | ILE79 |
| A | PRO120 |
| A | GLY122 |
| A | SER123 |
| A | GLY124 |
| A | LYS125 |
| A | THR126 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 500 |
| Chain | Residue |
| B | PRO120 |
| B | THR121 |
| B | GLY122 |
| B | SER123 |
| B | GLY124 |
| B | LYS125 |
| B | THR126 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 C 501 |
| Chain | Residue |
| C | PRO120 |
| C | GLY122 |
| C | SER123 |
| C | GLY124 |
| C | LYS125 |
| C | THR126 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 C 502 |
| Chain | Residue |
| C | GLY80 |
| C | GLN81 |
| C | GLU82 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 D 501 |
| Chain | Residue |
| D | PRO120 |
| D | GLY122 |
| D | SER123 |
| D | GLY124 |
| D | LYS125 |
| D | THR126 |
| E | PRO302 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 E 501 |
| Chain | Residue |
| E | PRO120 |
| E | GLY122 |
| E | SER123 |
| E | GLY124 |
| E | LYS125 |
| E | THR126 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 F 501 |
| Chain | Residue |
| F | PRO120 |
| F | GLY122 |
| F | SER123 |
| F | GLY124 |
| F | LYS125 |
| F | THR126 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 42 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00175","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19914167","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23622246","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
