3NKE
High resolution structure of the C-terminal domain CRISP-associated protein Cas1 from Escherichia coli str. K-12
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003676 | molecular_function | nucleic acid binding |
| A | 0004519 | molecular_function | endonuclease activity |
| A | 0004520 | molecular_function | DNA endonuclease activity |
| A | 0043571 | biological_process | maintenance of CRISPR repeat elements |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051607 | biological_process | defense response to virus |
| B | 0003676 | molecular_function | nucleic acid binding |
| B | 0004519 | molecular_function | endonuclease activity |
| B | 0004520 | molecular_function | DNA endonuclease activity |
| B | 0043571 | biological_process | maintenance of CRISPR repeat elements |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051607 | biological_process | defense response to virus |
| C | 0003676 | molecular_function | nucleic acid binding |
| C | 0004519 | molecular_function | endonuclease activity |
| C | 0004520 | molecular_function | DNA endonuclease activity |
| C | 0043571 | biological_process | maintenance of CRISPR repeat elements |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051607 | biological_process | defense response to virus |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 602 |
| Chain | Residue |
| A | ARG163 |
| A | THR184 |
| A | HOH348 |
| A | HOH970 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 603 |
| Chain | Residue |
| A | ARG112 |
| A | SER133 |
| A | GLU135 |
| B | ARG245 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO3 A 401 |
| Chain | Residue |
| C | GLN155 |
| C | HOH368 |
| A | LYS154 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1 |
| Chain | Residue |
| A | HOH22 |
| A | ARG245 |
| A | ARG248 |
| A | ARG252 |
| C | ARG112 |
| C | ARG138 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 3 |
| Chain | Residue |
| A | ARG131 |
| A | ARG132 |
| A | HOH297 |
| C | ARG256 |
| C | SER257 |
| C | HOH335 |
| C | HOH607 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 5 |
| Chain | Residue |
| A | GLU242 |
| A | PRO243 |
| A | ASP244 |
| A | ARG245 |
| A | HOH447 |
| A | HOH455 |
| A | HOH693 |
| B | LYS259 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 701 |
| Chain | Residue |
| B | ARG138 |
| B | HIS208 |
| B | THR209 |
| B | HOH370 |
| C | ARG248 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO C 601 |
| Chain | Residue |
| C | GLN178 |
| C | GLU242 |
| C | PRO243 |
| C | ASP244 |
| C | ARG245 |
| C | HOH464 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO3 C 401 |
| Chain | Residue |
| A | ARG131 |
| C | SER257 |
| C | SER258 |
| C | HOH492 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 C 2 |
| Chain | Residue |
| B | ARG112 |
| B | ARG138 |
| B | HOH423 |
| C | ARG245 |
| C | ARG248 |
| C | ARG252 |
| C | HOH349 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 C 4 |
| Chain | Residue |
| C | ARG163 |
| C | THR184 |
| C | TYR188 |
| C | LYS224 |
| C | HOH864 |
| C | HOH944 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:26503043, ECO:0007744|PDB:5DS5 |
| Chain | Residue | Details |
| A | GLU141 | |
| A | ASP221 | |
| B | GLU141 | |
| B | ASP221 | |
| C | GLU141 | |
| C | ASP221 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:26503043 |
| Chain | Residue | Details |
| A | HIS208 | |
| B | HIS208 | |
| C | HIS208 |
