3N5F
Crystal Structure of L-N-carbamoylase from Geobacillus stearothermophilus CECT43
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| A | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
| A | 0030145 | molecular_function | manganese ion binding |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050538 | molecular_function | N-carbamoyl-L-amino-acid hydrolase activity |
| A | 0050897 | molecular_function | cobalt ion binding |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| B | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
| B | 0030145 | molecular_function | manganese ion binding |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050538 | molecular_function | N-carbamoyl-L-amino-acid hydrolase activity |
| B | 0050897 | molecular_function | cobalt ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE IPA A 409 |
| Chain | Residue |
| A | GLY227 |
| B | THR257 |
| B | PRO351 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CO A 410 |
| Chain | Residue |
| A | HIS79 |
| A | ASP90 |
| A | GLU124 |
| A | HIS189 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE IPA B 409 |
| Chain | Residue |
| B | THR306 |
| B | LEU50 |
| B | ARG303 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CAC B 410 |
| Chain | Residue |
| A | HIS225 |
| A | ASN273 |
| B | ALA354 |
| B | ALA355 |
| B | HIS380 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CO B 411 |
| Chain | Residue |
| B | HIS79 |
| B | ASP90 |
| B | GLU124 |
| B | HIS189 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22904279, ECO:0007744|PDB:3N5F |
| Chain | Residue | Details |
| A | HIS79 | |
| A | HIS189 | |
| B | HIS79 | |
| B | HIS189 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q8VXY9 |
| Chain | Residue | Details |
| A | ASP90 | |
| A | GLU125 | |
| A | HIS380 | |
| B | ASP90 | |
| B | GLU125 | |
| B | HIS380 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22904279 |
| Chain | Residue | Details |
| A | HIS225 | |
| A | ASN273 | |
| A | ARG286 | |
| B | HIS225 | |
| B | ASN273 | |
| B | ARG286 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | SITE: Necessary for dimerization => ECO:0000269|PubMed:22904279 |
| Chain | Residue | Details |
| A | ARG234 | |
| B | ARG234 |
