5EBU
Aerococcus viridans L-lactate oxidase Y215F 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 |
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 | 23 |
Details | binding site for residue FMN A 400 |
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 | PYR401 |
A | HOH520 |
A | HOH523 |
A | ILE94 |
A | ALA95 |
A | SER122 |
A | GLN144 |
A | TYR146 |
A | THR172 |
A | LYS241 |
site_id | AC2 |
Number of Residues | 9 |
Details | binding site for residue PYR A 401 |
Chain | Residue |
A | TYR40 |
A | TYR124 |
A | TYR146 |
A | ARG181 |
A | LEU211 |
A | PHE215 |
A | HIS265 |
A | ARG268 |
A | FMN400 |
site_id | AC3 |
Number of Residues | 22 |
Details | binding site for residue FMN B 400 |
Chain | Residue |
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 | PYR401 |
B | HOH510 |
B | HOH512 |
B | HOH532 |
site_id | AC4 |
Number of Residues | 8 |
Details | binding site for residue PYR B 401 |
Chain | Residue |
B | TYR40 |
B | TYR124 |
B | TYR146 |
B | ARG181 |
B | LEU211 |
B | HIS265 |
B | ARG268 |
B | FMN400 |
site_id | AC5 |
Number of Residues | 22 |
Details | binding site for residue FMN C 400 |
Chain | Residue |
C | ILE41 |
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 | PYR401 |
C | HOH505 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue PYR C 401 |
Chain | Residue |
C | TYR40 |
C | TYR124 |
C | TYR146 |
C | ARG181 |
C | HIS265 |
C | ARG268 |
C | FMN400 |
site_id | AC7 |
Number of Residues | 25 |
Details | binding site for residue FMN D 400 |
Chain | Residue |
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 | PYR401 |
D | HOH502 |
D | HOH512 |
D | TYR40 |
D | ILE41 |
D | ALA92 |
D | PRO93 |
D | ILE94 |
D | ALA95 |
D | SER122 |
D | GLN144 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue PYR D 401 |
Chain | Residue |
D | TYR40 |
D | TYR146 |
D | ARG181 |
D | HIS265 |
D | ARG268 |
D | FMN400 |
site_id | AC9 |
Number of Residues | 24 |
Details | binding site for residue FMN E 400 |
Chain | Residue |
E | ILE41 |
E | ALA92 |
E | PRO93 |
E | ILE94 |
E | ALA95 |
E | SER122 |
E | GLN144 |
E | TYR146 |
E | THR172 |
E | LYS241 |
E | SER263 |
E | HIS265 |
E | GLY266 |
E | ARG268 |
E | ASP296 |
E | SER297 |
E | GLY298 |
E | VAL299 |
E | ARG300 |
E | GLY319 |
E | ARG320 |
E | PYR401 |
E | HOH501 |
E | HOH511 |
site_id | AD1 |
Number of Residues | 7 |
Details | binding site for residue PYR E 401 |
Chain | Residue |
E | TYR40 |
E | TYR146 |
E | ARG181 |
E | LEU211 |
E | HIS265 |
E | ARG268 |
E | FMN400 |
site_id | AD2 |
Number of Residues | 22 |
Details | binding site for residue FMN F 400 |
Chain | Residue |
F | ILE41 |
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 | PYR401 |
F | HOH504 |
F | HOH531 |
site_id | AD3 |
Number of Residues | 8 |
Details | binding site for residue PYR F 401 |
Chain | Residue |
F | TYR40 |
F | TYR124 |
F | TYR146 |
F | ARG181 |
F | LEU211 |
F | HIS265 |
F | ARG268 |
F | FMN400 |
site_id | AD4 |
Number of Residues | 22 |
Details | binding site for residue FMN G 400 |
Chain | Residue |
G | ILE41 |
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 | PYR401 |
G | HOH515 |
G | HOH525 |
site_id | AD5 |
Number of Residues | 8 |
Details | binding site for residue PYR G 401 |
Chain | Residue |
G | TYR40 |
G | ALA95 |
G | TYR124 |
G | TYR146 |
G | ARG181 |
G | HIS265 |
G | ARG268 |
G | FMN400 |
site_id | AD6 |
Number of Residues | 24 |
Details | binding site for residue FMN H 400 |
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 | VAL299 |
H | ARG300 |
H | GLY319 |
H | ARG320 |
H | PYR401 |
H | HOH517 |
H | HOH519 |
site_id | AD7 |
Number of Residues | 6 |
Details | binding site for residue PYR H 401 |
Chain | Residue |
H | TYR40 |
H | TYR146 |
H | ARG181 |
H | HIS265 |
H | ARG268 |
H | FMN400 |
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 | 2136 |
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 | 46 |
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 | 6 |
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 |