5FBD
S1 nuclease from Aspergillus oryzae in complex with phosphate and 2'-deoxycytidine
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003676 | molecular_function | nucleic acid binding |
A | 0004518 | molecular_function | nuclease activity |
A | 0004519 | molecular_function | endonuclease activity |
A | 0005575 | cellular_component | cellular_component |
A | 0006308 | biological_process | DNA catabolic process |
A | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
A | 0046872 | molecular_function | metal ion binding |
Functional Information from PROSITE/UniProt
site_id | PS00136 |
Number of Residues | 12 |
Details | SUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. STVLDDGLayiN |
Chain | Residue | Details |
A | SER237-ASN248 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:28036383, ECO:0007744|PDB:5FB9, ECO:0007744|PDB:5FBA, ECO:0007744|PDB:5FBB, ECO:0007744|PDB:5FBC, ECO:0007744|PDB:5FBD, ECO:0007744|PDB:5FBF, ECO:0007744|PDB:5FBG |
Chain | Residue | Details |
A | TRP21 | |
A | HIS26 | |
A | HIS80 | |
A | HIS135 | |
A | ASP139 | |
A | HIS145 | |
A | HIS168 | |
A | ASP172 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:28036383, ECO:0007744|PDB:5FBD, ECO:0007744|PDB:5FBF |
Chain | Residue | Details |
A | ASP65 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P24289 |
Chain | Residue | Details |
A | GLY93 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | SITE: Important for catalytic activity => ECO:0000269|PubMed:28036383 |
Chain | Residue | Details |
A | ASP65 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | SITE: Important for catalytic activity => ECO:0000250|UniProtKB:P24289 |
Chain | Residue | Details |
A | LYS68 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:28036383, ECO:0007744|PDB:5FB9, ECO:0007744|PDB:5FBB, ECO:0007744|PDB:5FBC, ECO:0007744|PDB:5FBD, ECO:0007744|PDB:5FBF, ECO:0007744|PDB:5FBG |
Chain | Residue | Details |
A | ASN112 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498 |
Chain | Residue | Details |
A | ASN122 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:28036383, ECO:0007744|PDB:5FB9, ECO:0007744|PDB:5FBA, ECO:0007744|PDB:5FBB, ECO:0007744|PDB:5FBC, ECO:0007744|PDB:5FBF, ECO:0007744|PDB:5FBG |
Chain | Residue | Details |
A | ASN248 |