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 | glutamate N-acetyltransferase activity |
A | 0006526 | biological_process | arginine biosynthetic process |
B | 0004358 | molecular_function | glutamate N-acetyltransferase activity |
B | 0006526 | biological_process | arginine biosynthetic process |
C | 0004358 | molecular_function | glutamate N-acetyltransferase activity |
C | 0006526 | biological_process | arginine biosynthetic process |
D | 0004358 | molecular_function | glutamate N-acetyltransferase activity |
D | 0006526 | biological_process | arginine biosynthetic process |
E | 0004358 | molecular_function | glutamate N-acetyltransferase activity |
E | 0006526 | biological_process | arginine biosynthetic process |
F | 0004358 | molecular_function | glutamate N-acetyltransferase activity |
F | 0006526 | biological_process | arginine biosynthetic process |
G | 0004358 | molecular_function | glutamate N-acetyltransferase activity |
G | 0006526 | biological_process | arginine biosynthetic process |
H | 0004358 | molecular_function | glutamate N-acetyltransferase activity |
H | 0006526 | biological_process | 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 | 1 |
Details | ACT_SITE: Nucleophile |
Chain | Residue | Details |
F | THR181 | |
D | TH5181 | |
H | TH5181 | |
E | THR148 | |
E | LYS170 | |
G | THR148 | |
G | LYS170 | |
C | LYS170 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:21796301 |
Chain | Residue | Details |
F | THR181 | |
F | GLU260 | |
F | ASN388 | |
F | THR393 | |
D | TH5181 | |
D | GLU260 | |
D | ASN388 | |
D | THR393 | |
H | TH5181 | |
H | GLU260 | |
H | ASN388 | |
H | THR393 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | SITE: Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole |
Chain | Residue | Details |
A | GLY112 | |
C | GLY112 | |
E | GLY112 | |
G | GLY112 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | SITE: Cleavage; by autolysis |
Chain | Residue | Details |
A | ALA180 | |
C | ALA180 | |
E | ALA180 | |
G | ALA180 |