2GB3
Crystal structure of Aspartate aminotransferase (tm1698) from Thermotoga maritima at 2.50 A resolution
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0006520 | biological_process | amino acid metabolic process |
A | 0008483 | molecular_function | transaminase activity |
A | 0009058 | biological_process | biosynthetic process |
A | 0030170 | molecular_function | pyridoxal phosphate binding |
B | 0003824 | molecular_function | catalytic activity |
B | 0006520 | biological_process | amino acid metabolic process |
B | 0008483 | molecular_function | transaminase activity |
B | 0009058 | biological_process | biosynthetic process |
B | 0030170 | molecular_function | pyridoxal phosphate binding |
C | 0003824 | molecular_function | catalytic activity |
C | 0006520 | biological_process | amino acid metabolic process |
C | 0008483 | molecular_function | transaminase activity |
C | 0009058 | biological_process | biosynthetic process |
C | 0030170 | molecular_function | pyridoxal phosphate binding |
D | 0003824 | molecular_function | catalytic activity |
D | 0006520 | biological_process | amino acid metabolic process |
D | 0008483 | molecular_function | transaminase activity |
D | 0009058 | biological_process | biosynthetic process |
D | 0030170 | molecular_function | pyridoxal phosphate binding |
E | 0003824 | molecular_function | catalytic activity |
E | 0006520 | biological_process | amino acid metabolic process |
E | 0008483 | molecular_function | transaminase activity |
E | 0009058 | biological_process | biosynthetic process |
E | 0030170 | molecular_function | pyridoxal phosphate binding |
F | 0003824 | molecular_function | catalytic activity |
F | 0006520 | biological_process | amino acid metabolic process |
F | 0008483 | molecular_function | transaminase activity |
F | 0009058 | biological_process | biosynthetic process |
F | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PROSITE/UniProt
site_id | PS00105 |
Number of Residues | 14 |
Details | AA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SVSKkfSAcGARVG |
Chain | Residue | Details |
A | SER229-GLY242 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ay4 |
Chain | Residue | Details |
A | ASP201 | |
A | TYR124 | |
B | ALA67 |
site_id | CSA10 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ay4 |
Chain | Residue | Details |
D | HIS65 |
site_id | CSA11 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ay4 |
Chain | Residue | Details |
E | HIS65 |
site_id | CSA12 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ay4 |
Chain | Residue | Details |
F | HIS65 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ay4 |
Chain | Residue | Details |
A | ALA67 | |
B | ASP201 | |
B | TYR124 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ay4 |
Chain | Residue | Details |
D | ALA67 | |
C | ASP201 | |
C | TYR124 |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ay4 |
Chain | Residue | Details |
C | ALA67 | |
D | ASP201 | |
D | TYR124 |
site_id | CSA5 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ay4 |
Chain | Residue | Details |
F | ALA67 | |
E | ASP201 | |
E | TYR124 |
site_id | CSA6 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ay4 |
Chain | Residue | Details |
F | ASP201 | |
F | TYR124 | |
E | ALA67 |
site_id | CSA7 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ay4 |
Chain | Residue | Details |
A | HIS65 |
site_id | CSA8 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ay4 |
Chain | Residue | Details |
B | HIS65 |
site_id | CSA9 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ay4 |
Chain | Residue | Details |
C | HIS65 |