9ENN
L-amino acid oxidase 4 (HcLAAO4) from the fungus Hebeloma cylindrosporum in complex with N-epsilon-acetyl-L-lysine
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 | 0009063 | biological_process | amino acid catabolic process |
A | 0016491 | molecular_function | oxidoreductase activity |
B | 0001716 | molecular_function | L-amino-acid oxidase activity |
B | 0005576 | cellular_component | extracellular region |
B | 0009063 | biological_process | amino acid catabolic process |
B | 0016491 | molecular_function | oxidoreductase activity |
C | 0001716 | molecular_function | L-amino-acid oxidase activity |
C | 0005576 | cellular_component | extracellular region |
C | 0009063 | biological_process | amino acid catabolic process |
C | 0016491 | molecular_function | oxidoreductase activity |
D | 0001716 | molecular_function | L-amino-acid oxidase activity |
D | 0005576 | cellular_component | extracellular region |
D | 0009063 | biological_process | amino acid catabolic process |
D | 0016491 | molecular_function | oxidoreductase activity |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:39152524, ECO:0007744|PDB:9ENI, ECO:0007744|PDB:9ENK, ECO:0007744|PDB:9ENN |
Chain | Residue | Details |
A | GLY75 | |
B | GLY75 | |
C | GLY75 | |
D | GLY75 |
site_id | SWS_FT_FI2 |
Number of Residues | 20 |
Details | BINDING: BINDING => ECO:0000269|PubMed:39152524, ECO:0007744|PDB:9ENH, ECO:0007744|PDB:9ENI, ECO:0007744|PDB:9ENJ, ECO:0007744|PDB:9ENK, ECO:0007744|PDB:9ENN |
Chain | Residue | Details |
A | GLU94 | |
B | VAL560 | |
C | GLU94 | |
C | ARG102 | |
C | MET122 | |
C | VAL334 | |
C | VAL560 | |
D | GLU94 | |
D | ARG102 | |
D | MET122 | |
D | VAL334 | |
A | ARG102 | |
D | VAL560 | |
A | MET122 | |
A | VAL334 | |
A | VAL560 | |
B | GLU94 | |
B | ARG102 | |
B | MET122 | |
B | VAL334 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:39152524, ECO:0007744|PDB:9ENH, ECO:0007744|PDB:9ENN |
Chain | Residue | Details |
A | ALA95 | |
B | ALA95 | |
C | ALA95 | |
D | ALA95 |
site_id | SWS_FT_FI4 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:39152524, ECO:0007744|PDB:9ENK |
Chain | Residue | Details |
A | ARG123 | |
D | ARG123 | |
D | TYR457 | |
D | ALA558 | |
A | TYR457 | |
A | ALA558 | |
B | ARG123 | |
B | TYR457 | |
B | ALA558 | |
C | ARG123 | |
C | TYR457 | |
C | ALA558 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:39152524, ECO:0007744|PDB:9ENI, ECO:0007744|PDB:9ENJ, ECO:0007744|PDB:9ENK, ECO:0007744|PDB:9ENN |
Chain | Residue | Details |
A | GLU551 | |
B | GLU551 | |
C | GLU551 | |
D | GLU551 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:39152524, ECO:0007744|PDB:9ENH, ECO:0007744|PDB:9ENJ, ECO:0007744|PDB:9ENK, ECO:0007744|PDB:9ENN |
Chain | Residue | Details |
A | TRP559 | |
B | TRP559 | |
C | TRP559 | |
D | TRP559 |
site_id | SWS_FT_FI7 |
Number of Residues | 12 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:34459552 |
Chain | Residue | Details |
A | ASN54 | |
D | ASN54 | |
D | ASN193 | |
D | ASN331 | |
A | ASN193 | |
A | ASN331 | |
B | ASN54 | |
B | ASN193 | |
B | ASN331 | |
C | ASN54 | |
C | ASN193 | |
C | ASN331 |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:34459552 |
Chain | Residue | Details |
A | ASN164 | |
B | ASN164 | |
C | ASN164 | |
D | ASN164 |