2GGK
The mutant A302C of Agrobacterium radiobacter N-carbamoyl-D-amino-acid amidohydrolase
Replaces: 2FKVReplaces: 2BA5Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003837 | molecular_function | beta-ureidopropionase activity |
| A | 0006807 | biological_process | obsolete nitrogen compound metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0033396 | biological_process | beta-alanine biosynthetic process via 3-ureidopropionate |
| A | 0047417 | molecular_function | N-carbamoyl-D-amino acid hydrolase activity |
| B | 0003837 | molecular_function | beta-ureidopropionase activity |
| B | 0006807 | biological_process | obsolete nitrogen compound metabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0033396 | biological_process | beta-alanine biosynthetic process via 3-ureidopropionate |
| B | 0047417 | molecular_function | N-carbamoyl-D-amino acid hydrolase activity |
| C | 0003837 | molecular_function | beta-ureidopropionase activity |
| C | 0006807 | biological_process | obsolete nitrogen compound metabolic process |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0033396 | biological_process | beta-alanine biosynthetic process via 3-ureidopropionate |
| C | 0047417 | molecular_function | N-carbamoyl-D-amino acid hydrolase activity |
| D | 0003837 | molecular_function | beta-ureidopropionase activity |
| D | 0006807 | biological_process | obsolete nitrogen compound metabolic process |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0033396 | biological_process | beta-alanine biosynthetic process via 3-ureidopropionate |
| D | 0047417 | molecular_function | N-carbamoyl-D-amino acid hydrolase activity |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | ACT_SITE: ACT_SITE => ECO:0000305|PubMed:11237598 |
| Chain | Residue | Details |
| A | GLU47 | |
| A | LYS127 | |
| A | CYS172 | |
| B | GLU47 | |
| B | LYS127 | |
| B | CYS172 | |
| C | GLU47 | |
| C | LYS127 | |
| C | CYS172 | |
| D | GLU47 | |
| D | LYS127 | |
| D | CYS172 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 671 |
| Chain | Residue | Details |
| A | GLU47 | proton acceptor, proton donor |
| A | ASN110 | electrostatic stabiliser |
| A | LYS127 | electrostatic stabiliser |
| A | GLU146 | electrostatic stabiliser |
| A | CYS172 | nucleofuge, nucleophile, proton acceptor, proton donor |
| A | ASN197 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 671 |
| Chain | Residue | Details |
| B | GLU47 | proton acceptor, proton donor |
| B | ASN110 | electrostatic stabiliser |
| B | LYS127 | electrostatic stabiliser |
| B | GLU146 | electrostatic stabiliser |
| B | CYS172 | nucleofuge, nucleophile, proton acceptor, proton donor |
| B | ASN197 | electrostatic stabiliser |
| site_id | MCSA3 |
| Number of Residues | 6 |
| Details | M-CSA 671 |
| Chain | Residue | Details |
| C | GLU47 | proton acceptor, proton donor |
| C | ASN110 | electrostatic stabiliser |
| C | LYS127 | electrostatic stabiliser |
| C | GLU146 | electrostatic stabiliser |
| C | CYS172 | nucleofuge, nucleophile, proton acceptor, proton donor |
| C | ASN197 | electrostatic stabiliser |
| site_id | MCSA4 |
| Number of Residues | 6 |
| Details | M-CSA 671 |
| Chain | Residue | Details |
| D | GLU47 | proton acceptor, proton donor |
| D | ASN110 | electrostatic stabiliser |
| D | LYS127 | electrostatic stabiliser |
| D | GLU146 | electrostatic stabiliser |
| D | CYS172 | nucleofuge, nucleophile, proton acceptor, proton donor |
| D | ASN197 | electrostatic stabiliser |
