2E5V
Crystal structure of L-Aspartate Oxidase from hyperthermophilic archaeon Sulfolobus tokodaii
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008734 | molecular_function | L-aspartate oxidase activity |
| A | 0009435 | biological_process | NAD biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019363 | biological_process | pyridine nucleotide biosynthetic process |
| A | 0034628 | biological_process | 'de novo' NAD biosynthetic process from aspartate |
| A | 0044318 | molecular_function | L-aspartate:fumarate oxidoreductase activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0008734 | molecular_function | L-aspartate oxidase activity |
| B | 0009435 | biological_process | NAD biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019363 | biological_process | pyridine nucleotide biosynthetic process |
| B | 0034628 | biological_process | 'de novo' NAD biosynthetic process from aspartate |
| B | 0044318 | molecular_function | L-aspartate:fumarate oxidoreductase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 2001 |
| Chain | Residue |
| A | ARG348 |
| A | SER351 |
| A | FAD1002 |
| A | HOH2175 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 2002 |
| Chain | Residue |
| B | ARG348 |
| B | SER351 |
| B | FAD1001 |
| B | HOH2154 |
| site_id | AC3 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE FAD A 1002 |
| Chain | Residue |
| A | GLY6 |
| A | SER7 |
| A | GLY8 |
| A | ILE9 |
| A | ALA10 |
| A | SER29 |
| A | LYS30 |
| A | ARG31 |
| A | GLY35 |
| A | SER36 |
| A | THR37 |
| A | ALA40 |
| A | GLY42 |
| A | GLY43 |
| A | ASP139 |
| A | LEU141 |
| A | ALA171 |
| A | THR172 |
| A | SER183 |
| A | ASN188 |
| A | ASP191 |
| A | HIS313 |
| A | PHE314 |
| A | GLY336 |
| A | GLU337 |
| A | ARG348 |
| A | SER351 |
| A | SER353 |
| A | LEU354 |
| A | CL2001 |
| A | HOH2014 |
| A | HOH2024 |
| A | HOH2031 |
| A | HOH2038 |
| A | HOH2078 |
| A | ILE5 |
| site_id | AC4 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE FAD B 1001 |
| Chain | Residue |
| B | ILE5 |
| B | GLY6 |
| B | SER7 |
| B | GLY8 |
| B | ILE9 |
| B | ALA10 |
| B | SER29 |
| B | LYS30 |
| B | ARG31 |
| B | GLY35 |
| B | SER36 |
| B | THR37 |
| B | ALA40 |
| B | GLY42 |
| B | GLY43 |
| B | LEU141 |
| B | ALA171 |
| B | THR172 |
| B | GLY173 |
| B | SER183 |
| B | ASN188 |
| B | ASP191 |
| B | HIS313 |
| B | PHE314 |
| B | GLY336 |
| B | GLU337 |
| B | ARG348 |
| B | SER351 |
| B | SER353 |
| B | LEU354 |
| B | CL2002 |
| B | HOH2007 |
| B | HOH2021 |
| B | HOH2031 |
| B | HOH2032 |
| B | HOH2047 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P10902 |
| Chain | Residue | Details |
| A | ARG257 | |
| B | ARG257 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18226609, ECO:0007744|PDB:2E5V |
| Chain | Residue | Details |
| A | SER36 | |
| A | GLY42 | |
| A | ASP191 | |
| A | GLU337 | |
| A | SER353 | |
| B | SER7 | |
| B | SER29 | |
| B | SER36 | |
| B | GLY42 | |
| B | ASP191 | |
| B | GLU337 | |
| B | SER353 | |
| A | SER7 | |
| A | SER29 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | SITE: Important in orienting the L-aspartate substrate => ECO:0000250|UniProtKB:P10902 |
| Chain | Residue | Details |
| A | GLU102 | |
| B | GLU102 |
