6P7Q
Structure of E. coli MS115-1 NucC, 5'-pApA bound form
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0004519 | molecular_function | endonuclease activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0051607 | biological_process | defense response to virus |
B | 0000166 | molecular_function | nucleotide binding |
B | 0004519 | molecular_function | endonuclease activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0051607 | biological_process | defense response to virus |
C | 0000166 | molecular_function | nucleotide binding |
C | 0004519 | molecular_function | endonuclease activity |
C | 0046872 | molecular_function | metal ion binding |
C | 0051607 | biological_process | defense response to virus |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | binding site for residue CL A 301 |
Chain | Residue |
A | ARG126 |
A | HOH552 |
B | TRP160 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 9 |
Details | ACT_SITE: ACT_SITE => ECO:0000305|PubMed:31932164 |
Chain | Residue | Details |
A | ASN73 | |
A | GLU104 | |
A | LYS106 | |
B | ASN73 | |
B | GLU104 | |
B | LYS106 | |
C | ASN73 | |
C | GLU104 | |
C | LYS106 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:31932164, ECO:0007744|PDB:6P7O |
Chain | Residue | Details |
A | ASN73 | |
A | GLU104 | |
B | ASN73 | |
B | GLU104 | |
C | ASN73 | |
C | GLU104 |
site_id | SWS_FT_FI3 |
Number of Residues | 9 |
Details | SITE: Binds cAAA => ECO:0000269|PubMed:31932164, ECO:0007744|PDB:6P7P |
Chain | Residue | Details |
A | ARG53 | |
A | TYR81 | |
A | THR226 | |
B | ARG53 | |
B | TYR81 | |
B | THR226 | |
C | ARG53 | |
C | TYR81 | |
C | THR226 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | SITE: Gate loop latch => ECO:0000269|PubMed:31932164, ECO:0007744|PDB:6P7P |
Chain | Residue | Details |
A | HIS136 | |
A | TYR141 | |
B | HIS136 | |
B | TYR141 | |
C | HIS136 | |
C | TYR141 |