2YEP
STRUCTURE OF AN N-TERMINAL NUCLEOPHILE (NTN) HYDROLASE, OAT2, IN COMPLEX WITH GLUTAMATE
Replaces: 2W4NFunctional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004358 | molecular_function | L-glutamate N-acetyltransferase activity, acting on acetyl-L-ornithine as donor |
| A | 0006526 | biological_process | L-arginine biosynthetic process |
| B | 0004358 | molecular_function | L-glutamate N-acetyltransferase activity, acting on acetyl-L-ornithine as donor |
| B | 0006526 | biological_process | L-arginine biosynthetic process |
| C | 0004358 | molecular_function | L-glutamate N-acetyltransferase activity, acting on acetyl-L-ornithine as donor |
| C | 0006526 | biological_process | L-arginine biosynthetic process |
| D | 0004358 | molecular_function | L-glutamate N-acetyltransferase activity, acting on acetyl-L-ornithine as donor |
| D | 0006526 | biological_process | L-arginine biosynthetic process |
| E | 0004358 | molecular_function | L-glutamate N-acetyltransferase activity, acting on acetyl-L-ornithine as donor |
| E | 0006526 | biological_process | L-arginine biosynthetic process |
| F | 0004358 | molecular_function | L-glutamate N-acetyltransferase activity, acting on acetyl-L-ornithine as donor |
| F | 0006526 | biological_process | L-arginine biosynthetic process |
| G | 0004358 | molecular_function | L-glutamate N-acetyltransferase activity, acting on acetyl-L-ornithine as donor |
| G | 0006526 | biological_process | L-arginine biosynthetic process |
| H | 0004358 | molecular_function | L-glutamate N-acetyltransferase activity, acting on acetyl-L-ornithine as donor |
| H | 0006526 | biological_process | L-arginine biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GLU B 1601 |
| Chain | Residue |
| A | THR148 |
| B | THR393 |
| A | THR149 |
| A | ASP150 |
| A | LYS170 |
| A | GLY171 |
| A | VAL172 |
| A | GLY173 |
| B | TH5181 |
| B | GLU260 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GLU C 1602 |
| Chain | Residue |
| C | THR148 |
| C | THR149 |
| C | ASP150 |
| C | LYS170 |
| C | GLY171 |
| C | VAL172 |
| C | GLY173 |
| C | HOH2025 |
| D | TH5181 |
| D | GLU260 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT E 1181 |
| Chain | Residue |
| E | THR148 |
| E | THR149 |
| F | THR181 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT G 1181 |
| Chain | Residue |
| G | THR148 |
| G | LYS170 |
| G | GLY173 |
| G | HOH2037 |
| H | TH5181 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Site: {"description":"Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Site: {"description":"Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21796301","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile"} |
| Chain | Residue | Details |
