4CWM
High-glycosylation crystal structure of the bifunctional endonuclease (AtBFN2) from Arabidopsis thaliana
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 |
