1JS1
Crystal Structure of a new transcarbamylase from the anaerobic bacterium Bacteroides fragilis at 2.0 A resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| X | 0004585 | molecular_function | ornithine carbamoyltransferase activity |
| X | 0006520 | biological_process | amino acid metabolic process |
| X | 0006526 | biological_process | arginine biosynthetic process |
| X | 0016597 | molecular_function | amino acid binding |
| X | 0016740 | molecular_function | transferase activity |
| X | 0016743 | molecular_function | carboxyl- or carbamoyltransferase activity |
| X | 0019240 | biological_process | citrulline biosynthetic process |
| X | 0042450 | biological_process | arginine biosynthetic process via ornithine |
| Y | 0004585 | molecular_function | ornithine carbamoyltransferase activity |
| Y | 0006520 | biological_process | amino acid metabolic process |
| Y | 0006526 | biological_process | arginine biosynthetic process |
| Y | 0016597 | molecular_function | amino acid binding |
| Y | 0016740 | molecular_function | transferase activity |
| Y | 0016743 | molecular_function | carboxyl- or carbamoyltransferase activity |
| Y | 0019240 | biological_process | citrulline biosynthetic process |
| Y | 0042450 | biological_process | arginine biosynthetic process via ornithine |
| Z | 0004585 | molecular_function | ornithine carbamoyltransferase activity |
| Z | 0006520 | biological_process | amino acid metabolic process |
| Z | 0006526 | biological_process | arginine biosynthetic process |
| Z | 0016597 | molecular_function | amino acid binding |
| Z | 0016740 | molecular_function | transferase activity |
| Z | 0016743 | molecular_function | carboxyl- or carbamoyltransferase activity |
| Z | 0019240 | biological_process | citrulline biosynthetic process |
| Z | 0042450 | biological_process | arginine biosynthetic process via ornithine |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 X 501 |
| Chain | Residue |
| X | SER47 |
| X | LEU48 |
| X | ARG49 |
| X | THR50 |
| X | ARG110 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 Y 502 |
| Chain | Residue |
| Y | ARG110 |
| Y | SER47 |
| Y | LEU48 |
| Y | ARG49 |
| Y | THR50 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 Z 503 |
| Chain | Residue |
| Z | SER46 |
| Z | SER47 |
| Z | LEU48 |
| Z | ARG49 |
| Z | THR50 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 15 |
| Details | BINDING: in other chain => ECO:0000250|UniProtKB:E1WKT5 |
| Chain | Residue | Details |
| X | CYS274 | |
| X | ARG302 | |
| Y | SER47 | |
| Y | ARG110 | |
| Y | HIS147 | |
| Y | CYS274 | |
| Y | ARG302 | |
| Z | SER47 | |
| Z | ARG110 | |
| Z | HIS147 | |
| Z | CYS274 | |
| Z | ARG302 | |
| X | SER47 | |
| X | ARG110 | |
| X | HIS147 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 15 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:E1WKT5 |
| Chain | Residue | Details |
| Y | GLU142 | |
| Y | HIS176 | |
| Y | LYS236 | |
| Y | ARG278 | |
| Z | TRP75 | |
| Z | GLU142 | |
| Z | HIS176 | |
| Z | LYS236 | |
| Z | ARG278 | |
| X | TRP75 | |
| X | GLU142 | |
| X | HIS176 | |
| X | LYS236 | |
| X | ARG278 | |
| Y | TRP75 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | SITE: Key residue in conferring substrate specificity for N-succinyl-L-ornithine versus N-acetyl-L-ornithine => ECO:0000250|UniProtKB:E1WKT5 |
| Chain | Residue | Details |
| X | PRO90 | |
| Y | PRO90 | |
| Z | PRO90 |
