2E77
Crystal structure of L-lactate oxidase with pyruvate complex
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 FMN A 4512 |
| Chain | Residue |
| A | ILE41 |
| A | LYS241 |
| A | SER263 |
| A | HIS265 |
| A | GLY266 |
| A | ARG268 |
| A | ASP296 |
| A | SER297 |
| A | GLY298 |
| A | ARG300 |
| A | GLY319 |
| A | ALA92 |
| A | ARG320 |
| A | PYR4442 |
| A | HOH4529 |
| A | HOH4530 |
| A | HOH4550 |
| A | PRO93 |
| A | ILE94 |
| A | ALA95 |
| A | SER122 |
| A | GLN144 |
| A | TYR146 |
| A | THR172 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PYR A 4442 |
| Chain | Residue |
| A | TYR40 |
| A | ALA95 |
| A | TYR124 |
| A | TYR146 |
| A | ARG181 |
| A | TYR215 |
| A | HIS265 |
| A | ARG268 |
| A | FMN4512 |
| site_id | AC3 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE FMN B 1512 |
| Chain | Residue |
| B | ALA1092 |
| B | PRO1093 |
| B | ILE1094 |
| B | ALA1095 |
| B | SER1122 |
| B | GLN1144 |
| B | TYR1146 |
| B | THR1172 |
| B | LYS1241 |
| B | SER1263 |
| B | HIS1265 |
| B | GLY1266 |
| B | ARG1268 |
| B | ASP1296 |
| B | SER1297 |
| B | GLY1298 |
| B | ARG1300 |
| B | GLY1319 |
| B | ARG1320 |
| B | PYR1442 |
| B | HOH1515 |
| B | HOH1527 |
| B | HOH1566 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PYR B 1442 |
| Chain | Residue |
| B | TYR1040 |
| B | ALA1095 |
| B | TYR1124 |
| B | TYR1146 |
| B | ARG1181 |
| B | LEU1211 |
| B | TYR1215 |
| B | HIS1265 |
| B | ARG1268 |
| B | FMN1512 |
| site_id | AC5 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE FMN C 2512 |
| Chain | Residue |
| C | ILE2041 |
| C | ALA2092 |
| C | PRO2093 |
| C | ILE2094 |
| C | ALA2095 |
| C | SER2122 |
| C | GLN2144 |
| C | TYR2146 |
| C | THR2172 |
| C | LYS2241 |
| C | SER2263 |
| C | HIS2265 |
| C | GLY2266 |
| C | ARG2268 |
| C | ASP2296 |
| C | SER2297 |
| C | GLY2298 |
| C | ARG2300 |
| C | GLY2319 |
| C | ARG2320 |
| C | HOH2525 |
| C | HOH2527 |
| C | HOH2555 |
| site_id | AC6 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE FMN D 3512 |
| Chain | Residue |
| D | HIS3265 |
| D | GLY3266 |
| D | ARG3268 |
| D | ASP3296 |
| D | SER3297 |
| D | GLY3298 |
| D | ARG3300 |
| D | GLY3319 |
| D | ARG3320 |
| D | PYR3442 |
| D | HOH3534 |
| D | HOH3540 |
| D | HOH3542 |
| D | ALA3092 |
| D | PRO3093 |
| D | ILE3094 |
| D | ALA3095 |
| D | SER3122 |
| D | GLN3144 |
| D | TYR3146 |
| D | THR3172 |
| D | LYS3241 |
| D | SER3263 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PYR D 3442 |
| Chain | Residue |
| D | TYR3040 |
| D | ALA3095 |
| D | TYR3124 |
| D | TYR3146 |
| D | ARG3181 |
| D | TYR3215 |
| D | HIS3265 |
| D | ARG3268 |
| D | FMN3512 |
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 | 24 |
| 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 | 4 |
| 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 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 712 |
| Details | Domain: {"description":"FMN hydroxy acid dehydrogenase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00683","evidenceCode":"ECO:0000255"}]} |
| 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 | CSA2 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1fcb |
| Chain | Residue | Details |
| B | ASP1174 | |
| B | HIS1265 | |
| B | TYR1146 | |
| B | TYR1040 | |
| B | ARG1268 |
| site_id | CSA3 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1fcb |
| Chain | Residue | Details |
| C | HIS2265 | |
| C | ARG2268 | |
| C | ASP2174 | |
| C | TYR2040 | |
| C | TYR2146 |
| site_id | CSA4 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1fcb |
| Chain | Residue | Details |
| D | ARG3268 | |
| D | TYR3146 | |
| D | ASP3174 | |
| D | TYR3040 | |
| D | HIS3265 |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1fcb |
| Chain | Residue | Details |
| A | ARG268 | |
| A | HIS265 | |
| A | ASP174 | |
| A | TYR146 |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1fcb |
| Chain | Residue | Details |
| B | ASP1174 | |
| B | HIS1265 | |
| B | TYR1146 | |
| B | ARG1268 |
| site_id | CSA7 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1fcb |
| Chain | Residue | Details |
| C | HIS2265 | |
| C | ARG2268 | |
| C | ASP2174 | |
| C | TYR2146 |
| site_id | CSA8 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1fcb |
| Chain | Residue | Details |
| D | ARG3268 | |
| D | TYR3146 | |
| D | ASP3174 | |
| D | HIS3265 |
