Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004519 | molecular_function | endonuclease activity |
A | 0005102 | molecular_function | signaling receptor binding |
A | 0009617 | biological_process | response to bacterium |
A | 0019835 | biological_process | cytolysis |
B | 0004519 | molecular_function | endonuclease activity |
B | 0005102 | molecular_function | signaling receptor binding |
B | 0009617 | biological_process | response to bacterium |
B | 0019835 | biological_process | cytolysis |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 200 |
Chain | Residue |
A | HIS102 |
A | HIS127 |
A | HIS131 |
A | HOH2027 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN B 200 |
Chain | Residue |
B | HIS102 |
B | HIS127 |
B | HIS131 |
B | HOH2064 |
B | HOH2065 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | HIS102 | |
A | HIS127 | |
A | HIS131 | |
B | HIS102 | |
B | HIS127 | |
B | HIS131 | |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 7 |
Details | M-CSA 791 |
Chain | Residue | Details |
A | ARG5 | electrostatic stabiliser |
A | ARG96 | electrostatic stabiliser |
A | GLU100 | electrostatic stabiliser |
A | HIS102 | metal ligand |
A | ALA103 | increase nucleophilicity, proton acceptor, proton donor |
A | HIS127 | metal ligand |
A | HIS131 | metal ligand |
site_id | MCSA2 |
Number of Residues | 7 |
Details | M-CSA 791 |
Chain | Residue | Details |
B | ARG5 | electrostatic stabiliser |
B | ARG96 | electrostatic stabiliser |
B | GLU100 | electrostatic stabiliser |
B | HIS102 | metal ligand |
B | ALA103 | increase nucleophilicity, proton acceptor, proton donor |
B | HIS127 | metal ligand |
B | HIS131 | metal ligand |