2NLI
Crystal Structure of the complex between L-lactate oxidase and a substrate analogue at 1.59 angstrom resolution
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE FMN A 1375 |
| 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 | LAC1376 |
| A | PEO1377 |
| A | HOH1379 |
| A | HOH1395 |
| A | HOH1408 |
| A | ILE94 |
| A | ALA95 |
| A | SER122 |
| A | GLN144 |
| A | TYR146 |
| A | THR172 |
| A | LYS241 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE LAC A 1376 |
| Chain | Residue |
| A | TYR40 |
| A | ALA95 |
| A | TYR124 |
| A | TYR146 |
| A | THR176 |
| A | ARG268 |
| A | FMN1375 |
| A | PEO1377 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEO A 1377 |
| Chain | Residue |
| A | HIS265 |
| A | FMN1375 |
| A | LAC1376 |
| site_id | AC4 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE FMN B 2375 |
| Chain | Residue |
| B | ILE41 |
| 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 | VAL299 |
| B | ARG300 |
| B | GLY319 |
| B | ARG320 |
| B | LAC2376 |
| B | PEO2377 |
| B | HOH2379 |
| B | HOH2385 |
| B | HOH2394 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE LAC B 2376 |
| Chain | Residue |
| B | TYR40 |
| B | ALA95 |
| B | TYR146 |
| B | ARG268 |
| B | FMN2375 |
| B | PEO2377 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEO B 2377 |
| Chain | Residue |
| B | HIS265 |
| B | FMN2375 |
| B | LAC2376 |
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 | 2 |
| 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 | 10 |
| 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 | 14 |
| 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 | 8 |
| 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 | 2 |
| 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 | 1 |
| 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 | 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 | 4 |
| Details | Annotated By Reference To The Literature 1fcb |
| Chain | Residue | Details |
| A | ARG268 | |
| A | HIS265 | |
| A | ASP174 | |
| A | TYR146 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1fcb |
| Chain | Residue | Details |
| B | ARG268 | |
| B | HIS265 | |
| B | ASP174 | |
| B | TYR146 |
