6Q1H
Structure of P. aeruginosa ATCC27853 NucC, cAAA-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 |
E | 0000166 | molecular_function | nucleotide binding |
E | 0004519 | molecular_function | endonuclease activity |
E | 0046872 | molecular_function | metal ion binding |
E | 0051607 | biological_process | defense response to virus |
F | 0000166 | molecular_function | nucleotide binding |
F | 0004519 | molecular_function | endonuclease activity |
F | 0046872 | molecular_function | metal ion binding |
F | 0051607 | biological_process | defense response to virus |
G | 0000166 | molecular_function | nucleotide binding |
G | 0004519 | molecular_function | endonuclease activity |
G | 0046872 | molecular_function | metal ion binding |
G | 0051607 | biological_process | defense response to virus |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 18 |
Details | ACT_SITE: ACT_SITE => ECO:0000305|PubMed:31932164 |
Chain | Residue | Details |
A | ASN73 | |
E | ASN73 | |
E | GLU104 | |
E | LYS106 | |
F | ASN73 | |
F | GLU104 | |
F | LYS106 | |
G | ASN73 | |
G | GLU104 | |
G | LYS106 | |
A | GLU104 | |
A | LYS106 | |
B | ASN73 | |
B | GLU104 | |
B | LYS106 | |
C | ASN73 | |
C | GLU104 | |
C | LYS106 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:D7Y2H5 |
Chain | Residue | Details |
A | ASN73 | |
F | GLU104 | |
G | ASN73 | |
G | GLU104 | |
A | GLU104 | |
B | ASN73 | |
B | GLU104 | |
C | ASN73 | |
C | GLU104 | |
E | ASN73 | |
E | GLU104 | |
F | ASN73 |
site_id | SWS_FT_FI3 |
Number of Residues | 18 |
Details | SITE: Binds cAAA => ECO:0000269|PubMed:31932164, ECO:0007744|PDB:6Q1H |
Chain | Residue | Details |
A | ARG53 | |
E | ARG53 | |
E | TYR81 | |
E | THR226 | |
F | ARG53 | |
F | TYR81 | |
F | THR226 | |
G | ARG53 | |
G | TYR81 | |
G | THR226 | |
A | TYR81 | |
A | THR226 | |
B | ARG53 | |
B | TYR81 | |
B | THR226 | |
C | ARG53 | |
C | TYR81 | |
C | THR226 |
site_id | SWS_FT_FI4 |
Number of Residues | 12 |
Details | SITE: Gate loop latch => ECO:0000269|PubMed:31932164, ECO:0007744|PDB:6Q1H |
Chain | Residue | Details |
A | HIS136 | |
F | TYR141 | |
G | HIS136 | |
G | TYR141 | |
A | TYR141 | |
B | HIS136 | |
B | TYR141 | |
C | HIS136 | |
C | TYR141 | |
E | HIS136 | |
E | TYR141 | |
F | HIS136 |