4W7L
CRYSTAL STRUCTURE OF A DECOLORIZING PEROXIDASE (DYP) FROM AURICULARIA AURICULA-JUDAE. D168N MUTANT
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004601 | molecular_function | peroxidase activity |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005829 | cellular_component | cytosol |
| A | 0020037 | molecular_function | heme binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0098869 | biological_process | cellular oxidant detoxification |
| A | 0140825 | molecular_function | lactoperoxidase activity |
| B | 0004601 | molecular_function | peroxidase activity |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005829 | cellular_component | cytosol |
| B | 0020037 | molecular_function | heme binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0098869 | biological_process | cellular oxidant detoxification |
| B | 0140825 | molecular_function | lactoperoxidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | binding site for residue HEM A 501 |
| Chain | Residue |
| A | GLU162 |
| A | HIS304 |
| A | ILE305 |
| A | THR308 |
| A | ARG309 |
| A | ARG311 |
| A | ARG332 |
| A | LEU357 |
| A | PHE359 |
| A | PHE370 |
| A | ILE398 |
| A | PHE166 |
| A | HOH811 |
| A | HOH815 |
| A | HOH818 |
| A | HOH856 |
| A | HOH965 |
| A | LEU167 |
| A | ASN168 |
| A | GLY169 |
| A | ILE170 |
| A | ALA171 |
| A | GLN221 |
| A | ARG255 |
| site_id | AC2 |
| Number of Residues | 24 |
| Details | binding site for residue HEM B 501 |
| Chain | Residue |
| B | GLU162 |
| B | PHE166 |
| B | LEU167 |
| B | ASN168 |
| B | GLY169 |
| B | ILE170 |
| B | ALA171 |
| B | GLN221 |
| B | ARG255 |
| B | HIS304 |
| B | ILE305 |
| B | THR308 |
| B | ARG309 |
| B | ARG311 |
| B | ARG332 |
| B | LEU357 |
| B | PHE359 |
| B | PHE370 |
| B | ILE398 |
| B | HOH800 |
| B | HOH801 |
| B | HOH802 |
| B | HOH858 |
| B | HOH959 |
Functional Information from PROSITE/UniProt
| site_id | PS00059 |
| Number of Residues | 15 |
| Details | ADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEmFGFlngiAqpA |
| Chain | Residue | Details |
| A | GLY160-ALA174 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:23235158 |
| Chain | Residue | Details |
| A | ASN168 | |
| B | ASN168 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: axial binding residue => ECO:0000269|PubMed:23235158, ECO:0000269|PubMed:25495127, ECO:0000269|PubMed:25542606, ECO:0000269|DOI:10.1039/c6cy00539j, ECO:0000269|Ref.8, ECO:0007744|PDB:4AU9, ECO:0007744|PDB:4UZI, ECO:0007744|PDB:4W7J, ECO:0007744|PDB:4W7K, ECO:0007744|PDB:4W7L, ECO:0007744|PDB:4W7M, ECO:0007744|PDB:4W7N, ECO:0007744|PDB:4W7O, ECO:0007744|PDB:5AG0, ECO:0007744|PDB:5IKD, ECO:0007744|PDB:5IKG |
| Chain | Residue | Details |
| A | HIS304 | |
| B | HIS304 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:23235158, ECO:0000269|PubMed:25542606, ECO:0000269|Ref.8, ECO:0007744|PDB:4AU9, ECO:0007744|PDB:4UZI, ECO:0007744|PDB:5AG0, ECO:0007744|PDB:5AG1 |
| Chain | Residue | Details |
| A | ASN282 | |
| A | ASN349 | |
| A | ASN415 | |
| B | ASN282 | |
| B | ASN349 | |
| B | ASN415 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498 |
| Chain | Residue | Details |
| A | ASN322 | |
| B | ASN322 |
