4HCB
The metal-free form of crystal structure of E.coli ExoI-ssDNA complex
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 | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 501 |
Chain | Residue |
A | HIS430 |
A | GLN433 |
A | HOH675 |
B | THR436 |
B | GLU438 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 502 |
Chain | Residue |
B | HIS215 |
B | ARG256 |
A | LYS214 |
A | HIS215 |
A | ARG256 |
B | LYS214 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 503 |
Chain | Residue |
A | ARG148 |
A | ARG203 |
A | HOH791 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 A 504 |
Chain | Residue |
A | ARG106 |
A | SER233 |
A | MET235 |
A | LYS299 |
A | HOH641 |
A | HOH689 |
A | HOH759 |
A | HOH809 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 505 |
Chain | Residue |
A | PHE415 |
A | PRO416 |
A | GLY417 |
A | HOH777 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 501 |
Chain | Residue |
A | GLU438 |
B | HIS430 |
B | GLN433 |
B | HOH707 |
B | HOH818 |
B | HOH838 |
site_id | AC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL B 502 |
Chain | Residue |
A | GLN328 |
A | ASP332 |
B | PHE11 |
B | SER38 |
B | GLU39 |
B | LYS198 |
B | PHE205 |
B | HOH835 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 503 |
Chain | Residue |
B | ARG148 |
B | ARG203 |
B | ARG316 |
B | HOH640 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 B 504 |
Chain | Residue |
B | ARG106 |
B | SER233 |
B | LYS299 |
B | HOH779 |
B | HOH824 |
B | HOH825 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 505 |
Chain | Residue |
B | SER373 |
B | ASP374 |
B | HOH621 |
B | HOH704 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 506 |
Chain | Residue |
A | SER373 |
A | ASP374 |
B | HIS211 |
B | LYS216 |
B | HOH786 |
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 |