4JRQ
Crystal structure of E. coli Exonuclease I in complex with a 5cy-dA13 oligonucleotide
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000175 | molecular_function | 3'-5'-RNA exonuclease activity |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003676 | molecular_function | nucleic acid binding |
| A | 0003677 | molecular_function | DNA binding |
| A | 0003697 | molecular_function | single-stranded DNA binding |
| A | 0004527 | molecular_function | exonuclease activity |
| A | 0004529 | molecular_function | DNA exonuclease activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0006259 | biological_process | DNA metabolic process |
| A | 0006274 | biological_process | DNA replication termination |
| A | 0006281 | biological_process | DNA repair |
| A | 0006308 | biological_process | DNA catabolic process |
| A | 0008310 | molecular_function | single-stranded DNA 3'-5' DNA exonuclease activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051575 | molecular_function | 5'-deoxyribose-5-phosphate lyase activity |
| B | 0000175 | molecular_function | 3'-5'-RNA exonuclease activity |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003676 | molecular_function | nucleic acid binding |
| B | 0003677 | molecular_function | DNA binding |
| B | 0003697 | molecular_function | single-stranded DNA binding |
| B | 0004527 | molecular_function | exonuclease activity |
| B | 0004529 | molecular_function | DNA exonuclease activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0006259 | biological_process | DNA metabolic process |
| B | 0006274 | biological_process | DNA replication termination |
| B | 0006281 | biological_process | DNA repair |
| B | 0006308 | biological_process | DNA catabolic process |
| B | 0008310 | molecular_function | single-stranded DNA 3'-5' DNA exonuclease activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051575 | molecular_function | 5'-deoxyribose-5-phosphate lyase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 501 |
| Chain | Residue |
| A | MET235 |
| A | HIS302 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 502 |
| Chain | Residue |
| A | ARG148 |
| A | ARG203 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 503 |
| Chain | Residue |
| A | THR210 |
| A | HIS211 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 504 |
| Chain | Residue |
| A | PHE205 |
| A | ASP206 |
| A | PHE209 |
| A | PHE11 |
| A | SER38 |
| A | LYS198 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 505 |
| Chain | Residue |
| A | PHE209 |
| A | ARG212 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE SO4 A 506 |
| Chain | Residue |
| A | HIS130 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 507 |
| Chain | Residue |
| A | ASP139 |
| A | ARG142 |
| A | SER233 |
| A | GLY234 |
| A | MET235 |
| C | DA9 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 501 |
| Chain | Residue |
| A | HIS215 |
| A | MET218 |
| A | ARG256 |
| B | HIS215 |
| B | MET218 |
| B | ARG256 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 502 |
| Chain | Residue |
| B | HIS302 |
| B | LYS305 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11101894, ECO:0000269|PubMed:18219121, ECO:0000269|PubMed:18591666, ECO:0000269|PubMed:20018747, ECO:0000269|PubMed:23609540 |
| Chain | Residue | Details |
| A | ASP15 | |
| B | ASP15 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18219121 |
| Chain | Residue | Details |
| A | GLU17 | |
| A | ARG165 | |
| A | ASP186 | |
| B | GLU17 | |
| B | ARG165 | |
| B | ASP186 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | SITE: Interaction with single-stranded DNA => ECO:0000269|PubMed:23609540 |
| Chain | Residue | Details |
| A | THR18 | |
| A | PHE371 | |
| B | THR18 | |
| B | ILE66 | |
| B | ARG113 | |
| B | TYR124 | |
| B | TRP128 | |
| B | ARG142 | |
| B | LYS214 | |
| B | TYR284 | |
| B | TYR368 | |
| A | ILE66 | |
| B | PHE371 | |
| A | ARG113 | |
| A | TYR124 | |
| A | TRP128 | |
| A | ARG142 | |
| A | LYS214 | |
| A | TYR284 | |
| A | TYR368 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | SITE: Important for interaction with ssb => ECO:0000269|PubMed:18591666 |
| Chain | Residue | Details |
| A | ARG148 | |
| A | TYR207 | |
| A | GLN311 | |
| B | ARG148 | |
| B | TYR207 | |
| B | GLN311 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | SITE: Interaction with single-stranded DNA => ECO:0000269|PubMed:23609540, ECO:0007744|PDB:4HCC |
| Chain | Residue | Details |
| A | PHE164 | |
| A | ASN257 | |
| A | ASN304 | |
| B | PHE164 | |
| B | ASN257 | |
| B | ASN304 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | SITE: Important for activity => ECO:0000269|PubMed:23609540 |
| Chain | Residue | Details |
| A | HIS181 | |
| B | HIS181 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | SITE: Important for interaction with ssb => ECO:0000305|PubMed:20018747 |
| Chain | Residue | Details |
| A | ARG338 | |
| B | ARG338 |
