8AQ0
Crystal structure of L-N-Carbamoylase from Sinorhizobium meliloti mutant L217G/F329C
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050538 | molecular_function | N-carbamoyl-L-amino-acid hydrolase activity |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050538 | molecular_function | N-carbamoyl-L-amino-acid hydrolase activity |
Functional Information from PROSITE/UniProt
| site_id | PS00697 |
| Number of Residues | 9 |
| Details | DNA_LIGASE_A1 ATP-dependent DNA ligase AMP-binding site. QAKLDGMRA |
| Chain | Residue | Details |
| A | GLN296-ALA304 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q8VXY9 |
| Chain | Residue | Details |
| A | HIS87 | |
| A | ASP98 | |
| A | GLU133 | |
| A | HIS194 | |
| A | HIS230 | |
| A | ASN279 | |
| A | ARG292 | |
| A | HIS386 | |
| B | HIS87 | |
| B | ASP98 | |
| B | GLU133 | |
| B | HIS194 | |
| B | HIS230 | |
| B | ASN279 | |
| B | ARG292 | |
| B | HIS386 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | SITE: Necessary for dimerization => ECO:0000250|UniProtKB:Q53389 |
| Chain | Residue | Details |
| A | ARG239 | |
| B | ARG239 |
