Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003677 | molecular_function | DNA binding |
A | 0003824 | molecular_function | catalytic activity |
A | 0004518 | molecular_function | nuclease activity |
A | 0004519 | molecular_function | endonuclease activity |
A | 0006281 | biological_process | DNA repair |
B | 0003677 | molecular_function | DNA binding |
B | 0003824 | molecular_function | catalytic activity |
B | 0004518 | molecular_function | nuclease activity |
B | 0004519 | molecular_function | endonuclease activity |
B | 0006281 | biological_process | DNA repair |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue MG A 401 |
Chain | Residue |
A | GLU96 |
A | HOH509 |
A | HOH578 |
D | 3DR1 |
P | DC10 |
site_id | AC2 |
Number of Residues | 7 |
Details | binding site for residue EDO A 402 |
Chain | Residue |
A | HOH527 |
A | HOH611 |
A | HOH648 |
A | LEU44 |
A | TYR45 |
A | ASN277 |
A | HOH505 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue EDO B 401 |
Chain | Residue |
B | ASP189 |
B | PHE192 |
B | GLY239 |
B | PHE240 |
B | HOH552 |
Functional Information from PROSITE/UniProt
site_id | PS00726 |
Number of Residues | 10 |
Details | AP_NUCLEASE_F1_1 AP endonucleases family 1 signature 1. PDILCLQETK |
Chain | Residue | Details |
A | PRO89-LYS98 | |
site_id | PS00727 |
Number of Residues | 17 |
Details | AP_NUCLEASE_F1_2 AP endonucleases family 1 signature 2. DSFRHlypntpyaYTFW |
Chain | Residue | Details |
A | ASP251-TRP267 | |
site_id | PS00728 |
Number of Residues | 12 |
Details | AP_NUCLEASE_F1_3 AP endonucleases family 1 signature 3. NvGwRLDYfLlS |
Chain | Residue | Details |
A | ASN277-SER288 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | TYR171 | |
B | TYR171 | |
Chain | Residue | Details |
A | ASP210 | |
B | ASP210 | |
Chain | Residue | Details |
A | HIS309 | |
B | HIS309 | |
Chain | Residue | Details |
A | ASN68 | |
B | ASN212 | |
B | ASP308 | |
B | HIS309 | |
A | GLU96 | |
A | ASP210 | |
A | ASN212 | |
A | ASP308 | |
A | HIS309 | |
B | ASN68 | |
B | GLU96 | |
B | ASP210 | |
Chain | Residue | Details |
A | ASN212 | |
B | ASN212 | |
Chain | Residue | Details |
A | ASP283 | |
B | ASP283 | |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | SITE: Interaction with DNA substrate |
Chain | Residue | Details |
A | HIS309 | |
B | HIS309 | |
Chain | Residue | Details |
A | SER54 | |
B | SER54 | |
Chain | Residue | Details |
A | CYS65 | |
A | CYS93 | |
B | CYS65 | |
B | CYS93 | |
Chain | Residue | Details |
A | LYS197 | |
B | LYS197 | |
Chain | Residue | Details |
A | THR233 | |
B | THR233 | |
Chain | Residue | Details |
A | CYS310 | |
B | CYS310 | |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 8 |
Details | M-CSA 510 |
Chain | Residue | Details |
A | ASP70 | metal ligand |
A | GLU96 | metal ligand |
A | TYR171 | electrostatic stabiliser, metal ligand |
A | ASP210 | increase nucleophilicity, metal ligand, proton acceptor |
A | ASN212 | |
A | ASP283 | electrostatic stabiliser |
A | ASP308 | metal ligand |
A | HIS309 | electrostatic stabiliser, metal ligand |
site_id | MCSA2 |
Number of Residues | 8 |
Details | M-CSA 510 |
Chain | Residue | Details |
B | ASP70 | metal ligand |
B | GLU96 | metal ligand |
B | TYR171 | electrostatic stabiliser, metal ligand |
B | ASP210 | increase nucleophilicity, metal ligand, proton acceptor |
B | ASN212 | |
B | ASP283 | electrostatic stabiliser |
B | ASP308 | metal ligand |
B | HIS309 | electrostatic stabiliser, metal ligand |