7LAE
CRYSTAL STRUCTURE OF MYELOPEROXIDASE SUBFORM C (MPO) COMPLEX WITH Compound-4
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004601 | molecular_function | peroxidase activity |
| A | 0006979 | biological_process | response to oxidative stress |
| A | 0020037 | molecular_function | heme binding |
| B | 0004601 | molecular_function | peroxidase activity |
| B | 0006979 | biological_process | response to oxidative stress |
| B | 0020037 | molecular_function | heme binding |
| D | 0004601 | molecular_function | peroxidase activity |
| D | 0006979 | biological_process | response to oxidative stress |
| D | 0020037 | molecular_function | heme binding |
| E | 0004601 | molecular_function | peroxidase activity |
| E | 0006979 | biological_process | response to oxidative stress |
| E | 0020037 | molecular_function | heme binding |
Functional Information from PROSITE/UniProt
| site_id | PS00435 |
| Number of Residues | 11 |
| Details | PEROXIDASE_1 Peroxidases proximal heme-ligand signature. EMPELTSMHTL |
| Chain | Residue | Details |
| B | GLU242-LEU252 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| B | MET190 | |
| E | MET190 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: covalent => ECO:0000269|PubMed:23843990, ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, ECO:0007744|PDB:4EJX |
| Chain | Residue | Details |
| B | ASN189 | |
| B | THR337 | |
| B | LEU338 | |
| E | ASN189 | |
| E | THR337 | |
| E | LEU338 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: |
| Chain | Residue | Details |
| B | SER191 | |
| E | SER191 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10766826, ECO:0000269|PubMed:11705390, ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, ECO:0007744|PDB:1D2V, ECO:0007744|PDB:1D7W, ECO:0007744|PDB:1DNU, ECO:0007744|PDB:1DNW, ECO:0007744|PDB:1MHL |
| Chain | Residue | Details |
| B | GLU263 | |
| B | LYS265 | |
| B | LEU267 | |
| B | PRO269 | |
| E | GLU263 | |
| E | LYS265 | |
| E | LEU267 | |
| E | PRO269 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: axial binding residue => ECO:0000269|PubMed:23843990, ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, ECO:0007744|PDB:4EJX |
| Chain | Residue | Details |
| B | PRO431 | |
| E | PRO431 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | SITE: Transition state stabilizer |
| Chain | Residue | Details |
| B | TYR334 | |
| E | TYR334 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: Cysteine sulfenic acid (-SOH) => ECO:0000269|PubMed:7840679 |
| Chain | Residue | Details |
| B | GLU245 | |
| E | GLU245 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:20332087 |
| Chain | Residue | Details |
| B | LEU252 | |
| E | LEU252 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20332087, ECO:0000269|PubMed:23843990, ECO:0007744|PDB:4EJX |
| Chain | Residue | Details |
| B | VAL284 | |
| B | VAL320 | |
| E | VAL284 | |
| E | VAL320 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:20332087, ECO:0000269|PubMed:23843990, ECO:0007744|PDB:4EJX |
| Chain | Residue | Details |
| B | ARG412 | |
| E | ARG412 |
