4LRL
Structure of an Enterococcus Faecalis HD-domain protein complexed with dGTP and dTTP
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0006203 | biological_process | dGTP catabolic process |
A | 0008832 | molecular_function | dGTPase activity |
A | 0045088 | biological_process | regulation of innate immune response |
A | 0046872 | molecular_function | metal ion binding |
A | 0051607 | biological_process | defense response to virus |
B | 0000166 | molecular_function | nucleotide binding |
B | 0006203 | biological_process | dGTP catabolic process |
B | 0008832 | molecular_function | dGTPase activity |
B | 0045088 | biological_process | regulation of innate immune response |
B | 0046872 | molecular_function | metal ion binding |
B | 0051607 | biological_process | defense response to virus |
C | 0000166 | molecular_function | nucleotide binding |
C | 0006203 | biological_process | dGTP catabolic process |
C | 0008832 | molecular_function | dGTPase activity |
C | 0045088 | biological_process | regulation of innate immune response |
C | 0046872 | molecular_function | metal ion binding |
C | 0051607 | biological_process | defense response to virus |
D | 0000166 | molecular_function | nucleotide binding |
D | 0006203 | biological_process | dGTP catabolic process |
D | 0008832 | molecular_function | dGTPase activity |
D | 0045088 | biological_process | regulation of innate immune response |
D | 0046872 | molecular_function | metal ion binding |
D | 0051607 | biological_process | defense response to virus |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NI A 501 |
Chain | Residue |
A | HIS66 |
A | HIS110 |
A | ASP111 |
A | ASP183 |
A | HOH651 |
A | HOH801 |
site_id | AC2 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE DGT A 502 |
Chain | Residue |
A | ILE35 |
A | ASN36 |
A | GLN41 |
A | ARG44 |
A | PHE64 |
A | HOH841 |
B | PHE54 |
B | THR55 |
B | ARG326 |
B | LYS330 |
B | HOH729 |
B | HOH737 |
B | HOH780 |
A | LYS14 |
A | VAL15 |
A | PHE16 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE TRS A 503 |
Chain | Residue |
A | ASP318 |
A | ARG322 |
A | PHE356 |
A | TYR361 |
A | HOH796 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NI B 501 |
Chain | Residue |
B | HIS66 |
B | HIS110 |
B | ASP111 |
B | ASP183 |
B | HOH742 |
B | HOH786 |
site_id | AC5 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE DGT B 502 |
Chain | Residue |
A | PHE54 |
A | THR55 |
A | VAL247 |
A | ARG326 |
A | LYS330 |
A | HOH677 |
B | LYS14 |
B | VAL15 |
B | PHE16 |
B | ASN36 |
B | GLN41 |
B | ARG44 |
B | PHE64 |
B | TTP503 |
B | HOH749 |
site_id | AC6 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE TTP B 503 |
Chain | Residue |
A | THR55 |
A | PHE56 |
A | GLN241 |
A | HIS245 |
A | HOH630 |
A | HOH652 |
A | HOH677 |
A | HOH729 |
A | HOH764 |
A | HOH815 |
B | VAL15 |
B | ARG17 |
B | DGT502 |
D | ARG206 |
D | ARG209 |
D | ASN223 |
D | HOH702 |
site_id | AC7 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE MLI B 504 |
Chain | Residue |
B | GLU7 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE TRS B 505 |
Chain | Residue |
B | ASP318 |
B | PHE356 |
B | HOH787 |
site_id | AC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE TRS B 506 |
Chain | Residue |
B | GLN135 |
B | PHE288 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NI C 501 |
Chain | Residue |
C | HIS66 |
C | HIS110 |
C | ASP111 |
C | ASP183 |
C | HOH747 |
C | HOH756 |
site_id | BC2 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE DGT C 502 |
Chain | Residue |
C | LYS14 |
C | VAL15 |
C | PHE16 |
C | ILE35 |
C | ASN36 |
C | GLN41 |
C | ARG44 |
C | PHE64 |
D | PHE54 |
D | THR55 |
D | VAL247 |
D | ARG326 |
D | LYS330 |
D | LYS422 |
D | HOH675 |
D | HOH716 |
D | HOH718 |
site_id | BC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MLI C 503 |
Chain | Residue |
C | VAL354 |
C | GLY355 |
C | PHE356 |
C | TYR361 |
C | HOH730 |
site_id | BC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NI D 501 |
Chain | Residue |
D | HIS66 |
D | HIS110 |
D | ASP111 |
D | ASP183 |
D | HOH698 |
D | HOH725 |
site_id | BC5 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE DGT D 502 |
Chain | Residue |
C | PHE54 |
C | THR55 |
C | VAL247 |
C | ARG326 |
C | LYS330 |
C | LYS422 |
C | HOH713 |
C | HOH724 |
D | LYS14 |
D | VAL15 |
D | PHE16 |
D | ASN36 |
D | GLN41 |
D | ARG44 |
D | PHE64 |
D | TTP503 |
D | HOH601 |
site_id | BC6 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE TTP D 503 |
Chain | Residue |
B | ARG206 |
B | ARG209 |
B | HOH664 |
C | THR55 |
C | PHE56 |
C | GLN241 |
C | HIS245 |
C | HOH641 |
C | HOH699 |
C | HOH711 |
D | VAL15 |
D | ARG17 |
D | DGT502 |
D | HOH601 |