1LGA
CRYSTALLOGRAPHIC REFINEMENT OF LIGNIN PEROXIDASE AT 2 ANGSTROMS
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 | 0006979 | biological_process | response to oxidative stress |
| A | 0016690 | molecular_function | diarylpropane 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 | 0098869 | biological_process | cellular oxidant detoxification |
| B | 0000302 | biological_process | response to reactive oxygen species |
| B | 0004601 | molecular_function | peroxidase activity |
| B | 0006979 | biological_process | response to oxidative stress |
| B | 0016690 | molecular_function | diarylpropane peroxidase activity |
| B | 0020037 | molecular_function | heme binding |
| B | 0034599 | biological_process | cellular response to oxidative stress |
| B | 0042744 | biological_process | hydrogen peroxide catabolic process |
| B | 0046274 | biological_process | lignin catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from PDB Data
| site_id | HPA |
| Number of Residues | 1 |
| Details | RESIDUE IN CHAIN A THAT H-BONDS WITH PROXIMAL HIS 176 |
| Chain | Residue |
| A | ASP238 |
| site_id | HPB |
| Number of Residues | 1 |
| Details | RESIDUE IN CHAIN B THAT H-BONDS WITH PROXIMAL HIS 176 |
| Chain | Residue |
| B | ASP238 |
| site_id | PBA |
| Number of Residues | 3 |
| Details | DISTAL RESIDUES IN CHAIN A FORMING THE PEROXIDE BINDING POCKET. THIS IS ANALOGOUS TO THE ARG-TRP-HIS FOUND IN CYTOCHROME C PEROXIDASE |
| Chain | Residue |
| A | ARG43 |
| A | PHE46 |
| A | HIS47 |
| site_id | PBB |
| Number of Residues | 3 |
| Details | DISTAL RESIDUES IN CHAIN B FORMING THE PEROXIDE BINDING POCKET. THIS IS ANALOGOUS TO THE ARG-TRP-HIS FOUND IN CYTOCHROME C PEROXIDASE |
| Chain | Residue |
| B | ARG43 |
| B | PHE46 |
| B | HIS47 |
| site_id | PHA |
| Number of Residues | 1 |
| Details | RESIDUES BOUND TO PROXIMAL HEME LIGAND, CHAIN A |
| Chain | Residue |
| A | HIS176 |
| site_id | PHB |
| Number of Residues | 1 |
| Details | RESIDUES BOUND TO PROXIMAL HEME LIGAND, CHAIN B |
| Chain | Residue |
| B | HIS176 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| A | HIS47 | |
| B | HIS47 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 18 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASP48 | |
| A | THR196 | |
| A | ILE199 | |
| A | ASP201 | |
| B | ASP48 | |
| B | GLY66 | |
| B | ASP68 | |
| B | SER70 | |
| B | SER177 | |
| B | ASP194 | |
| B | THR196 | |
| B | ILE199 | |
| B | ASP201 | |
| A | GLY66 | |
| A | ASP68 | |
| A | SER70 | |
| A | SER177 | |
| A | ASP194 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: axial binding residue |
| Chain | Residue | Details |
| A | HIS176 | |
| B | HIS176 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | SITE: Transition state stabilizer |
| Chain | Residue | Details |
| A | ARG43 | |
| B | ARG43 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: 3-hydroxytryptophan => ECO:0000269|PubMed:10024453 |
| Chain | Residue | Details |
| A | TRP171 | |
| B | TRP171 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| A | ASN257 | |
| B | ASN257 |
