4CXV
Structure of bifunctional endonuclease (AtBFN2) in complex with phosphate.
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000014 | molecular_function | single-stranded DNA endodeoxyribonuclease activity |
A | 0003676 | molecular_function | nucleic acid binding |
A | 0004519 | molecular_function | endonuclease activity |
A | 0004521 | molecular_function | RNA endonuclease activity |
A | 0006308 | biological_process | DNA catabolic process |
A | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
A | 0043765 | molecular_function | T/G mismatch-specific endonuclease activity |
A | 0046872 | molecular_function | metal ion binding |
A | 1990238 | molecular_function | double-stranded DNA endonuclease activity |
B | 0000014 | molecular_function | single-stranded DNA endodeoxyribonuclease activity |
B | 0003676 | molecular_function | nucleic acid binding |
B | 0004519 | molecular_function | endonuclease activity |
B | 0004521 | molecular_function | RNA endonuclease activity |
B | 0006308 | biological_process | DNA catabolic process |
B | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
B | 0043765 | molecular_function | T/G mismatch-specific endonuclease activity |
B | 0046872 | molecular_function | metal ion binding |
B | 1990238 | molecular_function | double-stranded DNA endonuclease activity |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:25157844, ECO:0000269|DOI:10.1016/j.bcab.2013.03.006, ECO:0007744|PDB:3W52, ECO:0007744|PDB:4CWM, ECO:0007744|PDB:4CXO, ECO:0007744|PDB:4CXP, ECO:0007744|PDB:4CXV |
Chain | Residue | Details |
A | TRP1 | |
B | HIS6 | |
B | HIS58 | |
B | HIS120 | |
B | ASP124 | |
B | HIS130 | |
B | HIS154 | |
B | ASP158 | |
A | HIS6 | |
A | HIS58 | |
A | HIS120 | |
A | ASP124 | |
A | HIS130 | |
A | HIS154 | |
A | ASP158 | |
B | TRP1 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:25157844, ECO:0007744|PDB:4CWM, ECO:0007744|PDB:4CXO, ECO:0007744|PDB:4CXP, ECO:0007744|PDB:4CXV |
Chain | Residue | Details |
A | ASP45 | |
B | ASP45 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P24289 |
Chain | Residue | Details |
A | SER67 | |
B | SER67 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:25157844, ECO:0007744|PDB:4CXO |
Chain | Residue | Details |
A | ASN91 | |
A | TYR109 | |
B | ASN91 | |
B | TYR109 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | SITE: Important for catalytic activity => ECO:0000250|UniProtKB:P24021 |
Chain | Residue | Details |
A | ASP45 | |
B | ASP45 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | SITE: Important for catalytic activity => ECO:0000250|UniProtKB:P24289 |
Chain | Residue | Details |
A | LYS48 | |
B | LYS48 |
site_id | SWS_FT_FI7 |
Number of Residues | 6 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:25157844, ECO:0000269|DOI:10.1016/j.bcab.2013.03.006, ECO:0007744|PDB:3W52, ECO:0007744|PDB:4CWM, ECO:0007744|PDB:4CXO, ECO:0007744|PDB:4CXP, ECO:0007744|PDB:4CXV |
Chain | Residue | Details |
A | ASN91 | |
A | ASN110 | |
A | ASN184 | |
B | ASN91 | |
B | ASN110 | |
B | ASN184 |