1OXO
ASPARTATE AMINOTRANSFERASE, H-ASP COMPLEX, OPEN CONFORMATION
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004069 | molecular_function | L-aspartate:2-oxoglutarate aminotransferase activity |
A | 0005739 | cellular_component | mitochondrion |
A | 0005759 | cellular_component | mitochondrial matrix |
A | 0006103 | biological_process | 2-oxoglutarate metabolic process |
A | 0006520 | biological_process | amino acid metabolic process |
A | 0006531 | biological_process | aspartate metabolic process |
A | 0006533 | biological_process | L-aspartate catabolic process |
A | 0006536 | biological_process | glutamate metabolic process |
A | 0008483 | molecular_function | transaminase activity |
A | 0009058 | biological_process | biosynthetic process |
A | 0016212 | molecular_function | kynurenine-oxoglutarate transaminase activity |
A | 0016740 | molecular_function | transferase activity |
A | 0030170 | molecular_function | pyridoxal phosphate binding |
A | 0042803 | molecular_function | protein homodimerization activity |
B | 0003824 | molecular_function | catalytic activity |
B | 0004069 | molecular_function | L-aspartate:2-oxoglutarate aminotransferase activity |
B | 0005739 | cellular_component | mitochondrion |
B | 0005759 | cellular_component | mitochondrial matrix |
B | 0006103 | biological_process | 2-oxoglutarate metabolic process |
B | 0006520 | biological_process | amino acid metabolic process |
B | 0006531 | biological_process | aspartate metabolic process |
B | 0006533 | biological_process | L-aspartate catabolic process |
B | 0006536 | biological_process | glutamate metabolic process |
B | 0008483 | molecular_function | transaminase activity |
B | 0009058 | biological_process | biosynthetic process |
B | 0016212 | molecular_function | kynurenine-oxoglutarate transaminase activity |
B | 0016740 | molecular_function | transferase activity |
B | 0030170 | molecular_function | pyridoxal phosphate binding |
B | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE IK2 A 411 |
Chain | Residue |
A | SER107 |
A | ARG266 |
A | HOH542 |
A | HOH589 |
A | HOH610 |
A | HOH611 |
B | TYR70 |
B | ARG292 |
A | GLY108 |
A | THR109 |
A | TRP140 |
A | ASN194 |
A | ASP222 |
A | TYR225 |
A | SER255 |
A | LYS258 |
site_id | AC2 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE IK2 B 411 |
Chain | Residue |
A | TYR70 |
B | SER107 |
B | GLY108 |
B | THR109 |
B | TRP140 |
B | HIS189 |
B | ASN194 |
B | ASP222 |
B | TYR225 |
B | SER255 |
B | LYS258 |
B | ARG266 |
B | HOH440 |
B | HOH487 |
B | HOH547 |
B | HOH591 |
B | HOH612 |
Functional Information from PROSITE/UniProt
site_id | PS00105 |
Number of Residues | 14 |
Details | AA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SYAKnmGLyGERAG |
Chain | Residue | Details |
A | SER255-GLY268 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | Binding site: {} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine"} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ay4 |
Chain | Residue | Details |
A | TRP140 | |
A | ASP222 | |
A | LYS258 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ay4 |
Chain | Residue | Details |
B | TRP140 | |
B | ASP222 | |
B | LYS258 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ay4 |
Chain | Residue | Details |
A | TRP140 | |
A | ASP222 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ay4 |
Chain | Residue | Details |
B | TRP140 | |
B | ASP222 |