5ABQ
CRYSTAL STRUCTURE ANALYSIS OF FUNGAL VERSATILE PEROXIDASE FROM PLEUROTUS ERYNGII. MUTANT VPi-SS. MUTATED RESIDUES T2K, A49C, A61C, D69S, T70D, S86E, A131K, D146T, Q202L, Q219K, H232E, Q239R, L288R, S301K, A308R,A309K AND A314R.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000302 | biological_process | response to reactive oxygen species |
| A | 0004601 | molecular_function | peroxidase activity |
| A | 0005576 | cellular_component | extracellular region |
| A | 0006979 | biological_process | response to oxidative stress |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016689 | molecular_function | manganese peroxidase activity |
| A | 0020037 | molecular_function | heme binding |
| A | 0034599 | biological_process | cellular response to oxidative stress |
| A | 0042744 | biological_process | hydrogen peroxide catabolic process |
| A | 0046274 | biological_process | lignin catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0052750 | molecular_function | reactive-black-5:hydrogen-peroxide oxidoreductase activity |
| A | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 1315 |
| Chain | Residue |
| A | ASP48 |
| A | GLY60 |
| A | ASP62 |
| A | SER64 |
| A | HOH2008 |
| A | HOH2011 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 1316 |
| Chain | Residue |
| A | VAL192 |
| A | ASP194 |
| A | SER170 |
| A | ASP187 |
| A | THR189 |
| site_id | AC3 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE HEM A 500 |
| Chain | Residue |
| A | HIS39 |
| A | GLU40 |
| A | LEU42 |
| A | ARG43 |
| A | PHE46 |
| A | PRO139 |
| A | GLU140 |
| A | PRO141 |
| A | LEU165 |
| A | LEU166 |
| A | SER168 |
| A | HIS169 |
| A | ALA172 |
| A | ALA173 |
| A | ALA174 |
| A | ASP175 |
| A | LYS176 |
| A | VAL177 |
| A | PHE186 |
| A | LEU228 |
| A | SER230 |
| A | HOH2006 |
| A | HOH2007 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 1317 |
| Chain | Residue |
| A | ASN96 |
| A | GLU140 |
| A | ASP143 |
| A | HOH2028 |
| A | HOH2030 |
| A | HOH2031 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CA A 1318 |
| Chain | Residue |
| A | GLY297 |
| A | HOH2062 |
Functional Information from PROSITE/UniProt
| site_id | PS00435 |
| Number of Residues | 11 |
| Details | PEROXIDASE_1 Peroxidases proximal heme-ligand signature. EVVWLLASHSI |
| Chain | Residue | Details |
| A | GLU161-ILE171 | |
| site_id | PS00436 |
| Number of Residues | 12 |
| Details | PEROXIDASE_2 Peroxidases active site signature. VHesLRLtFHDC |
| Chain | Residue | Details |
| A | VAL38-CYS49 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00297","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10012","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Tryptophan radical intermediate","evidences":[{"source":"PubMed","id":"16246366","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16246366","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 13 |
| Details | Binding site: {} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"axial binding residue"} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"PROSITE-ProRule","id":"PRU00297","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
