4CXO
bifunctional endonuclease in complex with ssDNA
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 | 0004518 | molecular_function | nuclease activity |
| A | 0004519 | molecular_function | endonuclease activity |
| A | 0004521 | molecular_function | RNA endonuclease activity |
| A | 0006308 | biological_process | DNA catabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| 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 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 7 |
| Details | Propeptide: {"description":"Removed in mature form","featureId":"PRO_0000445541","evidences":[{"source":"PubMed","id":"23620482","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 49 |
| Details | Region: {"description":"Substrate binding","evidences":[{"source":"PubMed","id":"25157844","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4CXO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4CXV","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25157844","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4CXV","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25157844","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2013","firstPage":"191","lastPage":"195","volume":"2","journal":"Biocatal. Agric. Biotechnol.","title":"Mechanistic insights to catalysis by a zinc-dependent bi-functional nuclease from Arabidopsis thaliana.","authors":["Chou T.-L.","Ko T.-P.","Ko C.-Y.","Lin T.-Y.","Guo R.-T.","Yu T.-F.","Chan H.-C.","Shaw J.-F.","Wang A.H.-J."],"citationCrossReferences":[{"database":"DOI","id":"10.1016/j.bcab.2013.03.006"}]}},{"source":"PDB","id":"3W52","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4CWM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4CXO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4CXP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4CXV","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25157844","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4CWM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4CXO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4CXP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4CXV","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P24289","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25157844","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4CXO","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Site: {"description":"Important for catalytic activity","evidences":[{"source":"UniProtKB","id":"P24021","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Site: {"description":"Important for catalytic activity","evidences":[{"source":"UniProtKB","id":"P24289","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 3 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"25157844","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2013","firstPage":"191","lastPage":"195","volume":"2","journal":"Biocatal. Agric. Biotechnol.","title":"Mechanistic insights to catalysis by a zinc-dependent bi-functional nuclease from Arabidopsis thaliana.","authors":["Chou T.-L.","Ko T.-P.","Ko C.-Y.","Lin T.-Y.","Guo R.-T.","Yu T.-F.","Chan H.-C.","Shaw J.-F.","Wang A.H.-J."],"citationCrossReferences":[{"database":"DOI","id":"10.1016/j.bcab.2013.03.006"}]}},{"source":"PDB","id":"3W52","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4CWM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4CXO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4CXP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4CXV","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
