4QQY
Crystal structure of T. fusca Cas3-ADP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003723 | molecular_function | RNA binding |
| A | 0003724 | molecular_function | RNA helicase activity |
| A | 0004386 | molecular_function | helicase activity |
| A | 0004518 | molecular_function | nuclease activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051607 | biological_process | defense response to virus |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0003723 | molecular_function | RNA binding |
| C | 0003724 | molecular_function | RNA helicase activity |
| C | 0004386 | molecular_function | helicase activity |
| C | 0004518 | molecular_function | nuclease activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051607 | biological_process | defense response to virus |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0003723 | molecular_function | RNA binding |
| E | 0003724 | molecular_function | RNA helicase activity |
| E | 0004386 | molecular_function | helicase activity |
| E | 0004518 | molecular_function | nuclease activity |
| E | 0005524 | molecular_function | ATP binding |
| E | 0016787 | molecular_function | hydrolase activity |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0051607 | biological_process | defense response to virus |
| G | 0000166 | molecular_function | nucleotide binding |
| G | 0003723 | molecular_function | RNA binding |
| G | 0003724 | molecular_function | RNA helicase activity |
| G | 0004386 | molecular_function | helicase activity |
| G | 0004518 | molecular_function | nuclease activity |
| G | 0005524 | molecular_function | ATP binding |
| G | 0016787 | molecular_function | hydrolase activity |
| G | 0046872 | molecular_function | metal ion binding |
| G | 0051607 | biological_process | defense response to virus |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE A 1001 |
| Chain | Residue |
| A | ASP84 |
| A | HIS115 |
| A | HIS149 |
| A | HIS150 |
| A | FE1002 |
| B | DA12 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE A 1002 |
| Chain | Residue |
| A | ASP215 |
| A | FE1001 |
| B | DA12 |
| A | HIS37 |
| A | HIS83 |
| A | ASP84 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ADP A 1003 |
| Chain | Residue |
| A | LEU277 |
| A | LYS279 |
| A | PRO280 |
| A | ASN281 |
| A | GLN284 |
| A | MET307 |
| A | GLY308 |
| A | GLU309 |
| A | GLY310 |
| A | GLU313 |
| A | ARG692 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE C 1001 |
| Chain | Residue |
| C | ASP84 |
| C | HIS115 |
| C | HIS149 |
| C | HIS150 |
| C | FE1002 |
| D | DA12 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE C 1002 |
| Chain | Residue |
| C | HIS37 |
| C | HIS83 |
| C | ASP84 |
| C | ASP215 |
| C | FE1001 |
| D | DA12 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ADP C 1003 |
| Chain | Residue |
| C | LEU277 |
| C | LYS279 |
| C | ASN281 |
| C | GLN284 |
| C | MET307 |
| C | GLY308 |
| C | GLU309 |
| C | GLY310 |
| C | GLU313 |
| C | ARG692 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE E 1001 |
| Chain | Residue |
| E | ASP84 |
| E | HIS115 |
| E | HIS149 |
| E | HIS150 |
| E | FE1002 |
| F | DA12 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE E 1002 |
| Chain | Residue |
| E | HIS37 |
| E | HIS83 |
| E | ASP84 |
| E | ASP215 |
| E | FE1001 |
| F | DA12 |
| site_id | AC9 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ADP E 1003 |
| Chain | Residue |
| E | LEU277 |
| E | SER278 |
| E | LYS279 |
| E | PRO280 |
| E | ASN281 |
| E | GLN284 |
| E | GLY308 |
| E | GLY310 |
| E | THR312 |
| E | GLU313 |
| E | ARG347 |
| E | ARG692 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE G 1001 |
| Chain | Residue |
| G | ASP84 |
| G | HIS115 |
| G | HIS149 |
| G | HIS150 |
| G | FE1002 |
| H | DA12 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FE G 1002 |
| Chain | Residue |
| G | HIS37 |
| G | HIS83 |
| G | ASP84 |
| G | LYS87 |
| G | ASP215 |
| G | FE1001 |
| H | DA12 |
| site_id | BC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ADP G 1003 |
| Chain | Residue |
| G | LEU277 |
| G | LYS279 |
| G | ASN281 |
| G | GLN284 |
| G | MET307 |
| G | GLY308 |
| G | GLU309 |
| G | GLY310 |
| G | GLU313 |
| G | ARG347 |
| G | ARG692 |






