1F8R
CRYSTAL STRUCTURE OF L-AMINO ACID OXIDASE FROM CALLOSELASMA RHODOSTOMA COMPLEXED WITH CITRATE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001716 | molecular_function | L-amino-acid oxidase activity |
| A | 0005576 | cellular_component | extracellular region |
| A | 0006915 | biological_process | apoptotic process |
| A | 0009063 | biological_process | amino acid catabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0031640 | biological_process | killing of cells of another organism |
| A | 0035821 | biological_process | modulation of process of another organism |
| A | 0042742 | biological_process | defense response to bacterium |
| A | 0090729 | molecular_function | toxin activity |
| A | 0106329 | molecular_function | L-phenylalaine oxidase activity |
| B | 0001716 | molecular_function | L-amino-acid oxidase activity |
| B | 0005576 | cellular_component | extracellular region |
| B | 0006915 | biological_process | apoptotic process |
| B | 0009063 | biological_process | amino acid catabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0031640 | biological_process | killing of cells of another organism |
| B | 0035821 | biological_process | modulation of process of another organism |
| B | 0042742 | biological_process | defense response to bacterium |
| B | 0090729 | molecular_function | toxin activity |
| B | 0106329 | molecular_function | L-phenylalaine oxidase activity |
| C | 0001716 | molecular_function | L-amino-acid oxidase activity |
| C | 0005576 | cellular_component | extracellular region |
| C | 0006915 | biological_process | apoptotic process |
| C | 0009063 | biological_process | amino acid catabolic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0031640 | biological_process | killing of cells of another organism |
| C | 0035821 | biological_process | modulation of process of another organism |
| C | 0042742 | biological_process | defense response to bacterium |
| C | 0090729 | molecular_function | toxin activity |
| C | 0106329 | molecular_function | L-phenylalaine oxidase activity |
| D | 0001716 | molecular_function | L-amino-acid oxidase activity |
| D | 0005576 | cellular_component | extracellular region |
| D | 0006915 | biological_process | apoptotic process |
| D | 0009063 | biological_process | amino acid catabolic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0031640 | biological_process | killing of cells of another organism |
| D | 0035821 | biological_process | modulation of process of another organism |
| D | 0042742 | biological_process | defense response to bacterium |
| D | 0090729 | molecular_function | toxin activity |
| D | 0106329 | molecular_function | L-phenylalaine oxidase activity |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020 |
| Chain | Residue | Details |
| A | MET43 | |
| B | GLY87 | |
| B | VAL261 | |
| B | GLU457 | |
| C | MET43 | |
| C | GLU63 | |
| C | ARG71 | |
| C | GLY87 | |
| C | VAL261 | |
| C | GLU457 | |
| D | MET43 | |
| A | GLU63 | |
| D | GLU63 | |
| D | ARG71 | |
| D | GLY87 | |
| D | VAL261 | |
| D | GLU457 | |
| A | ARG71 | |
| A | GLY87 | |
| A | VAL261 | |
| A | GLU457 | |
| B | MET43 | |
| B | GLU63 | |
| B | ARG71 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17046020, ECO:0007744|PDB:1F8R, ECO:0007744|PDB:1F8S, ECO:0007744|PDB:2IID |
| Chain | Residue | Details |
| A | ARG90 | |
| D | ARG90 | |
| D | HIS223 | |
| D | TYR372 | |
| A | HIS223 | |
| A | TYR372 | |
| B | ARG90 | |
| B | HIS223 | |
| B | TYR372 | |
| C | ARG90 | |
| C | HIS223 | |
| C | TYR372 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17046020, ECO:0007744|PDB:1F8S, ECO:0007744|PDB:2IID |
| Chain | Residue | Details |
| A | GLY464 | |
| B | GLY464 | |
| C | GLY464 | |
| D | GLY464 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:11453999 |
| Chain | Residue | Details |
| A | ASN172 | |
| A | ASN361 | |
| B | ASN172 | |
| B | ASN361 | |
| C | ASN172 | |
| C | ASN361 | |
| D | ASN172 | |
| D | ASN361 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 10944103, 17046020 |
| Chain | Residue | Details |
| A | HIS223 | |
| A | LYS326 |
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 555 |
| Chain | Residue | Details |
| A | HIS223 | proton acceptor, proton donor |
| A | LYS326 | proton acceptor |
| site_id | MCSA2 |
| Number of Residues | 2 |
| Details | M-CSA 555 |
| Chain | Residue | Details |
| B | HIS223 | proton acceptor, proton donor |
| B | LYS326 | proton acceptor |
| site_id | MCSA3 |
| Number of Residues | 2 |
| Details | M-CSA 555 |
| Chain | Residue | Details |
| C | HIS223 | proton acceptor, proton donor |
| C | LYS326 | proton acceptor |
| site_id | MCSA4 |
| Number of Residues | 2 |
| Details | M-CSA 555 |
| Chain | Residue | Details |
| D | HIS223 | proton acceptor, proton donor |
| D | LYS326 | proton acceptor |
