1JOG
Structure of HI0074 from Heamophilus Influenzae reveals the fold of a substrate binding domain of a nucleotidyltransferase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004518 | molecular_function | nuclease activity |
| A | 0004519 | molecular_function | endonuclease activity |
| A | 0016787 | molecular_function | hydrolase activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004518 | molecular_function | nuclease activity |
| B | 0004519 | molecular_function | endonuclease activity |
| B | 0016787 | molecular_function | hydrolase activity |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004518 | molecular_function | nuclease activity |
| C | 0004519 | molecular_function | endonuclease activity |
| C | 0016787 | molecular_function | hydrolase activity |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0004518 | molecular_function | nuclease activity |
| D | 0004519 | molecular_function | endonuclease activity |
| D | 0016787 | molecular_function | hydrolase activity |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 28 |
| Details | Motif: {"description":"RX(4)HXY motif","evidences":[{"source":"PubMed","id":"29555683","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Active site: {"evidences":[{"source":"UniProtKB","id":"A0A0B0QJR1","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"O-di-AMP-tyrosine","evidences":[{"source":"UniProtKB","id":"A0A0B0QJR1","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
