4RJE
Aerococcus viridans L-lactate oxidase mutant
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0010181 | molecular_function | FMN binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0010181 | molecular_function | FMN binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0010181 | molecular_function | FMN binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0010181 | molecular_function | FMN binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE FNR A 401 |
| Chain | Residue |
| A | ALA92 |
| A | SER263 |
| A | HIS265 |
| A | GLY266 |
| A | ARG268 |
| A | ASP296 |
| A | SER297 |
| A | GLY298 |
| A | VAL299 |
| A | ARG300 |
| A | GLY319 |
| A | PRO93 |
| A | ARG320 |
| A | PYR402 |
| A | HOH501 |
| A | HOH508 |
| A | HOH514 |
| A | ILE94 |
| A | GLY95 |
| A | SER122 |
| A | GLN144 |
| A | TYR146 |
| A | THR172 |
| A | LYS241 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PYR A 402 |
| Chain | Residue |
| A | TYR40 |
| A | TYR124 |
| A | TYR146 |
| A | ARG181 |
| A | LEU211 |
| A | TYR215 |
| A | HIS265 |
| A | ARG268 |
| A | FNR401 |
| A | HOH695 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 403 |
| Chain | Residue |
| A | GLU26 |
| A | LYS51 |
| A | HOH510 |
| A | HOH552 |
| site_id | AC4 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE FNR B 401 |
| Chain | Residue |
| B | ALA92 |
| B | PRO93 |
| B | ILE94 |
| B | GLY95 |
| B | SER122 |
| B | GLN144 |
| B | TYR146 |
| B | THR172 |
| B | LYS241 |
| B | SER263 |
| B | HIS265 |
| B | GLY266 |
| B | ARG268 |
| B | ASP296 |
| B | SER297 |
| B | GLY298 |
| B | ARG300 |
| B | GLY319 |
| B | ARG320 |
| B | PYR402 |
| B | HOH503 |
| B | HOH511 |
| B | HOH519 |
| B | HOH693 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PYR B 402 |
| Chain | Residue |
| B | TYR40 |
| B | TYR146 |
| B | ARG181 |
| B | LEU211 |
| B | TYR215 |
| B | HIS265 |
| B | ARG268 |
| B | FNR401 |
| B | HOH693 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 403 |
| Chain | Residue |
| B | GLU26 |
| B | LYS51 |
| B | HOH510 |
| B | HOH529 |
| site_id | AC7 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE FNR C 401 |
| Chain | Residue |
| C | ALA92 |
| C | PRO93 |
| C | ILE94 |
| C | GLY95 |
| C | SER122 |
| C | GLN144 |
| C | TYR146 |
| C | THR172 |
| C | LYS241 |
| C | SER263 |
| C | HIS265 |
| C | GLY266 |
| C | ARG268 |
| C | ASP296 |
| C | SER297 |
| C | GLY298 |
| C | VAL299 |
| C | ARG300 |
| C | GLY319 |
| C | ARG320 |
| C | PYR402 |
| C | HOH501 |
| C | HOH511 |
| C | HOH531 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PYR C 402 |
| Chain | Residue |
| C | TYR40 |
| C | TYR146 |
| C | ARG181 |
| C | LEU211 |
| C | HIS265 |
| C | ARG268 |
| C | FNR401 |
| C | HOH735 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO C 403 |
| Chain | Residue |
| C | GLU26 |
| C | LYS51 |
| C | HOH518 |
| C | HOH522 |
| site_id | BC1 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE FNR D 401 |
| Chain | Residue |
| D | ALA92 |
| D | PRO93 |
| D | ILE94 |
| D | GLY95 |
| D | SER122 |
| D | GLN144 |
| D | TYR146 |
| D | THR172 |
| D | LYS241 |
| D | SER263 |
| D | HIS265 |
| D | GLY266 |
| D | ARG268 |
| D | ASP296 |
| D | SER297 |
| D | GLY298 |
| D | VAL299 |
| D | ARG300 |
| D | GLY319 |
| D | ARG320 |
| D | PYR402 |
| D | HOH502 |
| D | HOH506 |
| D | HOH541 |
| D | HOH634 |
| site_id | BC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PYR D 402 |
| Chain | Residue |
| D | TYR40 |
| D | TYR124 |
| D | TYR146 |
| D | ARG181 |
| D | LEU211 |
| D | TYR215 |
| D | HIS265 |
| D | ARG268 |
| D | FNR401 |
| D | HOH634 |
Functional Information from PROSITE/UniProt
| site_id | PS00557 |
| Number of Residues | 7 |
| Details | FMN_HYDROXY_ACID_DH_1 FMN-dependent alpha-hydroxy acid dehydrogenases active site. SNHGARQ |
| Chain | Residue | Details |
| A | SER263-GLN269 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"27302031","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 23 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17517371","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25423902","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2E77","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4RJE","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 28 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17517371","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18367206","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2DU2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2E77","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2NLI","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17517371","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18367206","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2E77","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2NLI","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17517371","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2E77","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| Details | Site: {"description":"Is suggested to participate in control of opening/closing motions of the active-site lid in A.viridans LOX","evidences":[{"source":"PubMed","id":"27302031","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |






