1NBA
CRYSTAL STRUCTURE ANALYSIS, REFINEMENT AND ENZYMATIC REACTION MECHANISM OF N-CARBAMOYLSARCOSINE AMIDOHYDROLASE FROM ARTHROBACTER SP. AT 2.0 ANGSTROMS RESOLUTION
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006602 | biological_process | creatinine catabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0050127 | molecular_function | N-carbamoylsarcosine amidase activity |
| B | 0006602 | biological_process | creatinine catabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0050127 | molecular_function | N-carbamoylsarcosine amidase activity |
| C | 0006602 | biological_process | creatinine catabolic process |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0050127 | molecular_function | N-carbamoylsarcosine amidase activity |
| D | 0006602 | biological_process | creatinine catabolic process |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0050127 | molecular_function | N-carbamoylsarcosine amidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 400 |
| Chain | Residue |
| A | TRP56 |
| A | PHE63 |
| A | THR173 |
| A | CYS177 |
| A | ARG202 |
| A | HOH403 |
| A | HOH415 |
| B | LYS217 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 B 400 |
| Chain | Residue |
| B | TRP56 |
| B | PHE63 |
| B | THR173 |
| B | GLY176 |
| B | CYS177 |
| B | ARG202 |
| B | HOH411 |
| B | HOH427 |
| A | LYS217 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 C 400 |
| Chain | Residue |
| C | TRP56 |
| C | PHE63 |
| C | THR173 |
| C | CYS177 |
| C | ARG202 |
| C | HOH405 |
| C | HOH419 |
| D | LYS217 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 D 400 |
| Chain | Residue |
| C | LYS217 |
| D | TRP56 |
| D | PHE63 |
| D | THR173 |
| D | CYS177 |
| D | ARG202 |
| D | HOH413 |
| D | HOH430 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Nucleophile |
| Chain | Residue | Details |
| A | CYS177 | |
| B | CYS177 | |
| C | CYS177 | |
| D | CYS177 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | a catalytic site defined by CSA, PubMed 20366582, 1381445, 8913306 |
| Chain | Residue | Details |
| A | ALA172 | |
| A | ASP51 | |
| A | CYS177 | |
| A | THR173 | |
| A | LYS144 |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | a catalytic site defined by CSA, PubMed 20366582, 1381445, 8913306 |
| Chain | Residue | Details |
| B | ALA172 | |
| B | ASP51 | |
| B | CYS177 | |
| B | THR173 | |
| B | LYS144 |
| site_id | CSA3 |
| Number of Residues | 5 |
| Details | a catalytic site defined by CSA, PubMed 20366582, 1381445, 8913306 |
| Chain | Residue | Details |
| C | ALA172 | |
| C | ASP51 | |
| C | CYS177 | |
| C | THR173 | |
| C | LYS144 |
| site_id | CSA4 |
| Number of Residues | 5 |
| Details | a catalytic site defined by CSA, PubMed 20366582, 1381445, 8913306 |
| Chain | Residue | Details |
| D | ALA172 | |
| D | ASP51 | |
| D | CYS177 | |
| D | THR173 | |
| D | LYS144 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 25 |
| Chain | Residue | Details |
| A | ASP51 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | LYS144 | activator, electrostatic stabiliser, hydrogen bond donor |
| A | ALA172 | electrostatic stabiliser, hydrogen bond acceptor |
| A | THR173 | electrostatic stabiliser, hydrogen bond donor |
| A | CYS177 | covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 25 |
| Chain | Residue | Details |
| B | ASP51 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | LYS144 | activator, electrostatic stabiliser, hydrogen bond donor |
| B | ALA172 | electrostatic stabiliser, hydrogen bond acceptor |
| B | THR173 | electrostatic stabiliser, hydrogen bond donor |
| B | CYS177 | covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| site_id | MCSA3 |
| Number of Residues | 5 |
| Details | M-CSA 25 |
| Chain | Residue | Details |
| C | ASP51 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| C | LYS144 | activator, electrostatic stabiliser, hydrogen bond donor |
| C | ALA172 | electrostatic stabiliser, hydrogen bond acceptor |
| C | THR173 | electrostatic stabiliser, hydrogen bond donor |
| C | CYS177 | covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| site_id | MCSA4 |
| Number of Residues | 5 |
| Details | M-CSA 25 |
| Chain | Residue | Details |
| D | ASP51 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| D | LYS144 | activator, electrostatic stabiliser, hydrogen bond donor |
| D | ALA172 | electrostatic stabiliser, hydrogen bond acceptor |
| D | THR173 | electrostatic stabiliser, hydrogen bond donor |
| D | CYS177 | covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
