3ZS1
Human Myeloperoxidase inactivated by TX5
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 |
C | 0004601 | molecular_function | peroxidase activity |
C | 0006979 | biological_process | response to oxidative stress |
C | 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 |
Functional Information from PROSITE/UniProt
site_id | PS00435 |
Number of Residues | 11 |
Details | PEROXIDASE_1 Peroxidases proximal heme-ligand signature. EMPELTSMHTL |
Chain | Residue | Details |
C | GLU242-LEU252 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
C | MET190 | |
D | 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 |
C | ASN189 | |
C | THR337 | |
C | LEU338 | |
D | ASN189 | |
D | THR337 | |
D | LEU338 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: |
Chain | Residue | Details |
C | SER191 | |
D | 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 |
C | GLU263 | |
C | LYS265 | |
C | LEU267 | |
C | PRO269 | |
D | GLU263 | |
D | LYS265 | |
D | LEU267 | |
D | 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 |
C | PRO431 | |
D | PRO431 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | SITE: Transition state stabilizer |
Chain | Residue | Details |
C | TYR334 | |
D | TYR334 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: Cysteine sulfenic acid (-SOH) => ECO:0000269|PubMed:7840679 |
Chain | Residue | Details |
C | GLU245 | |
D | 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 |
C | LEU252 | |
D | 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 |
C | VAL284 | |
C | VAL320 | |
D | VAL284 | |
D | 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 |
C | ARG412 | |
D | ARG412 |