5HP4
Crystal structure bacteriohage T5 D15 flap endonuclease (D155K) pseudo-enzyme-product complex with DNA 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 | 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 | 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 | 0140640 | molecular_function | catalytic activity, acting on a nucleic acid |
| A | 1990238 | molecular_function | double-stranded DNA endonuclease activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | binding site for residue CA X 101 |
| Chain | Residue |
| A | HOH557 |
| A | HOH570 |
| X | DC15 |
| X | HOH216 |
| X | HOH220 |
| X | HOH221 |
| X | HOH223 |
| X | HOH236 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue NA X 102 |
| Chain | Residue |
| X | DT5 |
| X | DT7 |
| X | DA8 |
| X | HOH231 |
| X | HOH234 |
| X | DC4 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue K X 103 |
| Chain | Residue |
| A | MET199 |
| A | VAL209 |
| A | ILE212 |
| X | DT5 |
| X | HOH224 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 301 |
| Chain | Residue |
| A | GLU128 |
| A | ASP130 |
| A | HOH405 |
| A | HOH413 |
| A | HOH430 |
| A | HOH522 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 302 |
| Chain | Residue |
| A | THR28 |
| A | ASP68 |
| A | PHE112 |
| A | THR123 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04140, ECO:0000269|PubMed:10364212 |
| Chain | Residue | Details |
| A | LYS83 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04140, ECO:0000269|PubMed:27273516 |
| Chain | Residue | Details |
| A | ASP130 | |
| A | LYS155 | |
| A | ASP201 | |
| A | VAL209 | |
| A | ILE212 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04140, ECO:0000269|PubMed:15077103, ECO:0000269|PubMed:27273516, ECO:0000269|PubMed:8657312 |
| Chain | Residue | Details |
| A | ASP153 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 10 |
| Details | M-CSA 549 |
| Chain | Residue | Details |
| A | ASP26 | metal ligand |
| A | ASP204 | metal ligand |
| A | ASP68 | metal ligand |
| A | LYS83 | electrostatic stabiliser, proton shuttle (general acid/base) |
| A | ARG86 | electrostatic stabiliser |
| A | GLU128 | metal ligand |
| A | ASP131 | metal ligand |
| A | ASP153 | metal ligand |
| A | LYS155 | metal ligand |
| A | ASP201 | metal ligand |
