5HNK
Crystal structure of T5Fen in complex intact substrate and metal ions.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003677 | molecular_function | DNA binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004518 | molecular_function | nuclease activity |
| A | 0004519 | molecular_function | endonuclease activity |
| A | 0004527 | molecular_function | exonuclease activity |
| A | 0004529 | molecular_function | DNA exonuclease activity |
| A | 0006260 | biological_process | DNA replication |
| A | 0008409 | molecular_function | 5'-3' exonuclease activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| A | 0017108 | molecular_function | 5'-flap endonuclease activity |
| A | 0019034 | cellular_component | viral replication complex |
| A | 0019086 | biological_process | late viral transcription |
| A | 0033567 | biological_process | DNA replication, Okazaki fragment processing |
| A | 0035312 | molecular_function | 5'-3' DNA exonuclease activity |
| A | 0039693 | biological_process | viral DNA genome replication |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0048256 | molecular_function | flap endonuclease activity |
| A | 0051908 | molecular_function | double-stranded DNA 5'-3' DNA exonuclease activity |
| A | 1990238 | molecular_function | double-stranded DNA endonuclease activity |
| B | 0003677 | molecular_function | DNA binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004518 | molecular_function | nuclease activity |
| B | 0004519 | molecular_function | endonuclease activity |
| B | 0004527 | molecular_function | exonuclease activity |
| B | 0004529 | molecular_function | DNA exonuclease activity |
| B | 0006260 | biological_process | DNA replication |
| B | 0008409 | molecular_function | 5'-3' exonuclease activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| B | 0017108 | molecular_function | 5'-flap endonuclease activity |
| B | 0019034 | cellular_component | viral replication complex |
| B | 0019086 | biological_process | late viral transcription |
| B | 0033567 | biological_process | DNA replication, Okazaki fragment processing |
| B | 0035312 | molecular_function | 5'-3' DNA exonuclease activity |
| B | 0039693 | biological_process | viral DNA genome replication |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0048256 | molecular_function | flap endonuclease activity |
| B | 0051908 | molecular_function | double-stranded DNA 5'-3' DNA exonuclease activity |
| B | 1990238 | molecular_function | double-stranded DNA endonuclease activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue MG Y 101 |
| Chain | Residue |
| B | HOH409 |
| B | HOH423 |
| B | HOH450 |
| Y | DC6 |
| Y | HOH207 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue MG Y 102 |
| Chain | Residue |
| Y | HOH212 |
| Y | HOH218 |
| B | HOH462 |
| Y | DG7 |
| Y | HOH205 |
| Y | HOH208 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue K Y 103 |
| Chain | Residue |
| A | MET199 |
| A | VAL209 |
| Y | DC10 |
| Y | HOH211 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 301 |
| Chain | Residue |
| B | ASP87 |
| B | LYS280 |
| B | ASP284 |
| Y | DA1 |
| Y | DA3 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 146 |
| Details | Domain: {"description":"5'-3' exonuclease","evidences":[{"source":"HAMAP-Rule","id":"MF_04140","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 68 |
| Details | Region: {"description":"Helical arch","evidences":[{"source":"HAMAP-Rule","id":"MF_04140","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"27273516","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8657312","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 72 |
| Details | Region: {"description":"DNA-binding; H3TH","evidences":[{"source":"HAMAP-Rule","id":"MF_04140","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"27273516","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_04140","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10364212","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_04140","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"27273516","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_04140","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15077103","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27273516","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8657312","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
