5MFA
Crystal structure of human promyeloperoxidase (proMPO)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001878 | biological_process | response to yeast |
| A | 0002149 | biological_process | hypochlorous acid biosynthetic process |
| A | 0002679 | biological_process | respiratory burst involved in defense response |
| A | 0003682 | molecular_function | chromatin binding |
| A | 0004601 | molecular_function | peroxidase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005634 | cellular_component | nucleus |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005764 | cellular_component | lysosome |
| A | 0006952 | biological_process | defense response |
| A | 0006979 | biological_process | response to oxidative stress |
| A | 0008201 | molecular_function | heparin binding |
| A | 0009612 | biological_process | response to mechanical stimulus |
| A | 0019430 | biological_process | removal of superoxide radicals |
| A | 0020037 | molecular_function | heme binding |
| A | 0030141 | cellular_component | secretory granule |
| A | 0032094 | biological_process | response to food |
| A | 0032496 | biological_process | response to lipopolysaccharide |
| A | 0034374 | biological_process | low-density lipoprotein particle remodeling |
| A | 0035578 | cellular_component | azurophil granule lumen |
| A | 0042582 | cellular_component | azurophil granule |
| A | 0042742 | biological_process | defense response to bacterium |
| A | 0042744 | biological_process | hydrogen peroxide catabolic process |
| A | 0043066 | biological_process | negative regulation of apoptotic process |
| A | 0043231 | cellular_component | intracellular membrane-bounded organelle |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050832 | biological_process | defense response to fungus |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0097013 | cellular_component | phagocytic vesicle lumen |
| A | 1990268 | biological_process | response to gold nanoparticle |
Functional Information from PROSITE/UniProt
| site_id | PS00435 |
| Number of Residues | 11 |
| Details | PEROXIDASE_1 Peroxidases proximal heme-ligand signature. EMPELTSMHTL |
| Chain | Residue | Details |
| A | GLU408-LEU418 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| A | HIS261 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | BINDING: covalent => ECO:0000269|PubMed:23843990, ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, ECO:0007744|PDB:4EJX |
| Chain | Residue | Details |
| A | ASP260 | |
| A | GLU408 | |
| A | MET409 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASP262 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| 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 |
| A | THR334 | |
| A | PHE336 | |
| A | ASP338 | |
| A | SER340 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | BINDING: axial binding residue => ECO:0000269|PubMed:23843990, ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, ECO:0007744|PDB:4EJX |
| Chain | Residue | Details |
| A | HIS502 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | SITE: Transition state stabilizer |
| Chain | Residue | Details |
| A | ARG405 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | MOD_RES: Cysteine sulfenic acid (-SOH) => ECO:0000269|PubMed:7840679 |
| Chain | Residue | Details |
| A | CSO316 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952 |
| Chain | Residue | Details |
| A | ASN139 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:20332087 |
| Chain | Residue | Details |
| A | ASN323 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| 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 |
| A | ASN355 | |
| A | ASN391 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| 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 |
| A | ASN483 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:20332087 |
| Chain | Residue | Details |
| A | ASN729 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 601 |
| Chain | Residue | Details |
| A | HIS261 | proton shuttle (general acid/base) |
| A | ARG405 | electrostatic stabiliser |
