4JRP
Structure of E. coli Exonuclease I in complex with a 5cy-dT13 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 | 0004518 | molecular_function | nuclease activity |
| 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 | 0006974 | biological_process | DNA damage response |
| A | 0008310 | molecular_function | single-stranded DNA 3'-5' DNA exonuclease activity |
| A | 0016787 | molecular_function | hydrolase 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 | 0004518 | molecular_function | nuclease activity |
| 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 | 0006974 | biological_process | DNA damage response |
| B | 0008310 | molecular_function | single-stranded DNA 3'-5' DNA exonuclease activity |
| B | 0016787 | molecular_function | hydrolase 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 | 6 |
| Details | BINDING SITE FOR RESIDUE MG C 101 |
| Chain | Residue |
| A | ASP15 |
| A | HOH610 |
| A | HOH611 |
| A | HOH735 |
| C | DT12 |
| C | DT13 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 A 501 |
| Chain | Residue |
| A | ARG256 |
| A | HOH601 |
| B | HIS215 |
| B | ARG256 |
| B | HOH672 |
| B | HOH695 |
| A | LYS214 |
| A | HIS215 |
| A | MET218 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 A 502 |
| Chain | Residue |
| A | ARG106 |
| A | SER233 |
| A | MET235 |
| A | LYS299 |
| A | LEU300 |
| A | HIS302 |
| A | HOH644 |
| A | HOH720 |
| A | HOH746 |
| A | HOH749 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 503 |
| Chain | Residue |
| A | PHE415 |
| A | PRO416 |
| A | GLY417 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 504 |
| Chain | Residue |
| A | ARG148 |
| A | ARG203 |
| A | ARG316 |
| A | HOH682 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 505 |
| Chain | Residue |
| A | ARG35 |
| A | GLY44 |
| A | GLU45 |
| A | GLU47 |
| A | LEU91 |
| A | HOH740 |
| A | HOH741 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 506 |
| Chain | Residue |
| A | THR436 |
| A | PRO437 |
| A | GLU438 |
| B | HIS430 |
| B | GLN433 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 507 |
| Chain | Residue |
| A | HIS430 |
| A | GLN433 |
| A | HOH675 |
| B | THR436 |
| B | GLU438 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 501 |
| Chain | Residue |
| B | ARG148 |
| B | ARG203 |
| B | ALA393 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 502 |
| Chain | Residue |
| B | THR210 |
| B | HIS211 |
| B | LYS216 |
| B | ARG389 |
| B | ASN390 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 503 |
| Chain | Residue |
| B | HIS22 |
| B | PRO23 |
| B | ALA24 |
| B | LEU25 |
| B | HOH751 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 504 |
| Chain | Residue |
| B | ASN414 |
| B | PHE415 |
| B | PRO416 |
| B | GLY417 |
| B | HOH719 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 505 |
| Chain | Residue |
| B | ASN157 |
| B | SER163 |
| B | PHE164 |
| B | ARG165 |
| B | HIS168 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 506 |
| Chain | Residue |
| B | PRO228 |
| B | LEU334 |
| B | ARG338 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 507 |
| Chain | Residue |
| A | LYS216 |
| B | SER373 |
| B | ASP374 |
| B | HOH688 |
| site_id | BC7 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE SO4 B 508 |
| Chain | Residue |
| B | ARG200 |
| site_id | BC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 509 |
| Chain | Residue |
| B | GLN129 |
| B | LYS381 |
| B | HOH601 |
| B | HOH602 |
| D | 5CY0 |
| site_id | BC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE IPA B 510 |
| Chain | Residue |
| A | PHE439 |
| A | GLY442 |
| A | TYR443 |
| A | HOH690 |
| B | GLY442 |
| B | TYR443 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11101894","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18219121","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18591666","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20018747","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23609540","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18219121","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | Site: {"description":"Interaction with single-stranded DNA","evidences":[{"source":"PubMed","id":"23609540","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Site: {"description":"Important for interaction with ssb","evidences":[{"source":"PubMed","id":"18591666","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Site: {"description":"Interaction with single-stranded DNA","evidences":[{"source":"PubMed","id":"23609540","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4HCC","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Site: {"description":"Important for activity","evidences":[{"source":"PubMed","id":"23609540","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Site: {"description":"Important for interaction with ssb","evidences":[{"source":"PubMed","id":"20018747","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 153 |
| Details | Domain: {"description":"ExoI SH3-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU01120","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 117 |
| Details | Domain: {"description":"ExoI C-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU01121","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
