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 |