1KNP
E. coli L-aspartate oxidase: mutant R386L in complex with succinate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| 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 L-aspartate |
| A | 0044281 | biological_process | small molecule metabolic process |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 541 |
| Chain | Residue |
| A | THR353 |
| A | GLY355 |
| A | GLU375 |
| A | SER377 |
| A | HOH812 |
| site_id | AC2 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE FAD A 800 |
| Chain | Residue |
| A | ALA19 |
| A | SER37 |
| A | LYS38 |
| A | SER45 |
| A | THR46 |
| A | TYR48 |
| A | ALA49 |
| A | GLN50 |
| A | GLY51 |
| A | GLY52 |
| A | THR160 |
| A | ASN161 |
| A | ALA162 |
| A | ALA203 |
| A | THR204 |
| A | GLY205 |
| A | ASN216 |
| A | ASP223 |
| A | LEU257 |
| A | HIS351 |
| A | TYR352 |
| A | GLY374 |
| A | GLU375 |
| A | SER389 |
| A | SER391 |
| A | LEU392 |
| A | CYS395 |
| A | SIN801 |
| A | GLY15 |
| A | SER16 |
| A | GLY17 |
| A | ALA18 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SIN A 801 |
| Chain | Residue |
| A | GLY51 |
| A | GLU121 |
| A | HIS244 |
| A | THR259 |
| A | GLU260 |
| A | ARG290 |
| A | HIS351 |
| A | ALA388 |
| A | SER389 |
| A | SER391 |
| A | FAD800 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"11294641","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"11863440","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1KNP","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 15 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11863440","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KNP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1KNR","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11863440","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KNP","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Site: {"description":"Important in orienting the L-aspartate substrate","evidences":[{"source":"PubMed","id":"11294641","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 11863440 |
| Chain | Residue | Details |
| A | LEU386 | |
| A | ARG290 | |
| A | HIS351 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 739 |
| Chain | Residue | Details |
| A | GLU121 | electrostatic stabiliser, proton acceptor, steric role |
| A | HIS244 | electrostatic stabiliser |
| A | ARG290 | electrostatic stabiliser, proton acceptor, proton donor |
| A | HIS351 | electrostatic stabiliser |
| A | LEU386 | electrostatic stabiliser |
