2J6X
The crystal structure of lactate oxidase
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 |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0010181 | molecular_function | FMN binding |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0010181 | molecular_function | FMN binding |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0046872 | molecular_function | metal ion binding |
| G | 0000166 | molecular_function | nucleotide binding |
| G | 0010181 | molecular_function | FMN binding |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0046872 | molecular_function | metal ion binding |
| H | 0000166 | molecular_function | nucleotide binding |
| H | 0010181 | molecular_function | FMN binding |
| H | 0016491 | molecular_function | oxidoreductase activity |
| H | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D1376 |
| Chain | Residue |
| D | GLU229 |
| D | HIS233 |
| E | GLU229 |
| E | HIS233 |
| site_id | AC2 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE FMN A1375 |
| Chain | Residue |
| A | GLN144 |
| A | TYR146 |
| A | THR172 |
| A | LYS241 |
| A | SER263 |
| A | HIS265 |
| A | GLY266 |
| A | ARG268 |
| A | ASP296 |
| A | SER297 |
| A | GLY298 |
| A | ARG300 |
| A | GLY319 |
| A | ARG320 |
| A | HOH2033 |
| A | HOH2170 |
| A | HOH2197 |
| A | HOH2198 |
| A | HOH2199 |
| A | ILE41 |
| A | ALA92 |
| A | PRO93 |
| A | ILE94 |
| A | ALA95 |
| site_id | AC3 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE FMN B1375 |
| Chain | Residue |
| B | ALA92 |
| B | PRO93 |
| B | ILE94 |
| B | ALA95 |
| 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 | HOH2183 |
| B | HOH2184 |
| B | HOH2185 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE FMN C1375 |
| Chain | Residue |
| C | ALA92 |
| C | PRO93 |
| C | ILE94 |
| C | ALA95 |
| 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 | ARG300 |
| C | GLY319 |
| C | ARG320 |
| C | HOH2036 |
| C | HOH2169 |
| C | HOH2171 |
| site_id | AC5 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE FMN D1375 |
| Chain | Residue |
| D | ALA92 |
| D | PRO93 |
| D | ILE94 |
| D | ALA95 |
| 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 | ARG300 |
| D | GLY319 |
| D | ARG320 |
| D | HOH2143 |
| D | HOH2144 |
| D | HOH2145 |
| site_id | AC6 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE FMN E1375 |
| Chain | Residue |
| E | TYR146 |
| E | THR172 |
| E | LYS241 |
| E | SER263 |
| E | HIS265 |
| E | GLY266 |
| E | ARG268 |
| E | ASP296 |
| E | SER297 |
| E | GLY298 |
| E | ARG300 |
| E | GLY319 |
| E | ARG320 |
| E | HOH2024 |
| E | HOH2103 |
| E | HOH2132 |
| E | ALA92 |
| E | PRO93 |
| E | ILE94 |
| E | ALA95 |
| E | GLN144 |
| site_id | AC7 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE FMN F1375 |
| Chain | Residue |
| F | ILE41 |
| F | ALA92 |
| F | PRO93 |
| F | ILE94 |
| F | ALA95 |
| F | SER122 |
| F | GLN144 |
| F | TYR146 |
| F | THR172 |
| F | LYS241 |
| F | SER263 |
| F | HIS265 |
| F | GLY266 |
| F | ARG268 |
| F | ASP296 |
| F | SER297 |
| F | GLY298 |
| F | ARG300 |
| F | GLY319 |
| F | ARG320 |
| F | HOH2022 |
| F | HOH2114 |
| F | HOH2148 |
| site_id | AC8 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE FMN G1375 |
| Chain | Residue |
| G | ALA92 |
| G | PRO93 |
| G | ILE94 |
| G | ALA95 |
| G | SER122 |
| G | GLN144 |
| G | TYR146 |
| G | THR172 |
| G | LYS241 |
| G | SER263 |
| G | HIS265 |
| G | GLY266 |
| G | ARG268 |
| G | ASP296 |
| G | SER297 |
| G | GLY298 |
| G | ARG300 |
| G | GLY319 |
| G | ARG320 |
| G | HOH2123 |
| G | HOH2158 |
| site_id | AC9 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE FMN H1375 |
| Chain | Residue |
| H | ILE41 |
| H | ALA92 |
| H | PRO93 |
| H | ILE94 |
| H | ALA95 |
| H | SER122 |
| H | GLN144 |
| H | TYR146 |
| H | THR172 |
| H | LYS241 |
| H | SER263 |
| H | HIS265 |
| H | GLY266 |
| H | ARG268 |
| H | ASP296 |
| H | SER297 |
| H | GLY298 |
| H | ARG300 |
| H | GLY319 |
| H | ARG320 |
| H | HOH2136 |
| H | HOH2159 |
| H | HOH2160 |
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 | 1780 |
| Details | Domain: {"description":"FMN hydroxy acid dehydrogenase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00683","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"27302031","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 47 |
| 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_FI4 |
| Number of Residues | 56 |
| 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_FI5 |
| Number of Residues | 32 |
| 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_FI6 |
| Number of Residues | 8 |
| 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_FI7 |
| Number of Residues | 7 |
| 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 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1fcb |
| Chain | Residue | Details |
| A | TYR40 | |
| A | ARG268 | |
| A | ASP174 | |
| A | HIS265 | |
| A | TYR146 |
| site_id | CSA10 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1fcb |
| Chain | Residue | Details |
| B | ARG268 | |
| B | HIS265 | |
| B | ASP174 | |
| B | TYR146 |
| site_id | CSA11 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1fcb |
| Chain | Residue | Details |
| C | ARG268 | |
| C | HIS265 | |
| C | ASP174 | |
| C | TYR146 |
| site_id | CSA12 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1fcb |
| Chain | Residue | Details |
| D | ARG268 | |
| D | HIS265 | |
| D | ASP174 | |
| D | TYR146 |
| site_id | CSA13 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1fcb |
| Chain | Residue | Details |
| E | ARG268 | |
| E | HIS265 | |
| E | ASP174 | |
| E | TYR146 |
| site_id | CSA14 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1fcb |
| Chain | Residue | Details |
| F | ARG268 | |
| F | HIS265 | |
| F | ASP174 | |
| F | TYR146 |
| site_id | CSA15 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1fcb |
| Chain | Residue | Details |
| G | ARG268 | |
| G | HIS265 | |
| G | ASP174 | |
| G | TYR146 |
| site_id | CSA16 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1fcb |
| Chain | Residue | Details |
| H | ARG268 | |
| H | HIS265 | |
| H | ASP174 | |
| H | TYR146 |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1fcb |
| Chain | Residue | Details |
| B | TYR40 | |
| B | ARG268 | |
| B | ASP174 | |
| B | HIS265 | |
| B | TYR146 |
| site_id | CSA3 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1fcb |
| Chain | Residue | Details |
| C | TYR40 | |
| C | ARG268 | |
| C | ASP174 | |
| C | HIS265 | |
| C | TYR146 |
| site_id | CSA4 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1fcb |
| Chain | Residue | Details |
| D | TYR40 | |
| D | ARG268 | |
| D | ASP174 | |
| D | HIS265 | |
| D | TYR146 |
| site_id | CSA5 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1fcb |
| Chain | Residue | Details |
| E | TYR40 | |
| E | ARG268 | |
| E | ASP174 | |
| E | HIS265 | |
| E | TYR146 |
| site_id | CSA6 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1fcb |
| Chain | Residue | Details |
| F | TYR40 | |
| F | ARG268 | |
| F | ASP174 | |
| F | HIS265 | |
| F | TYR146 |
| site_id | CSA7 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1fcb |
| Chain | Residue | Details |
| G | TYR40 | |
| G | ARG268 | |
| G | ASP174 | |
| G | HIS265 | |
| G | TYR146 |
| site_id | CSA8 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1fcb |
| Chain | Residue | Details |
| H | TYR40 | |
| H | ARG268 | |
| H | ASP174 | |
| H | HIS265 | |
| H | TYR146 |
| site_id | CSA9 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1fcb |
| Chain | Residue | Details |
| A | ARG268 | |
| A | HIS265 | |
| A | ASP174 | |
| A | TYR146 |






