7Z53
Structure of native leukocyte myeloperoxidase in complex with a truncated version (SPIN truncated) of the Staphyloccal Peroxidase Inhibitor SPIN from Staphylococcus aureus
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 |
| G | 0004601 | molecular_function | peroxidase activity |
| G | 0006979 | biological_process | response to oxidative stress |
| G | 0020037 | molecular_function | heme binding |
| H | 0004601 | molecular_function | peroxidase activity |
| H | 0006979 | biological_process | response to oxidative stress |
| H | 0020037 | molecular_function | heme binding |
| I | 0004601 | molecular_function | peroxidase activity |
| I | 0006979 | biological_process | response to oxidative stress |
| I | 0020037 | molecular_function | heme binding |
| J | 0004601 | molecular_function | peroxidase activity |
| J | 0006979 | biological_process | response to oxidative stress |
| J | 0020037 | molecular_function | heme binding |
| M | 0004601 | molecular_function | peroxidase activity |
| M | 0006979 | biological_process | response to oxidative stress |
| M | 0020037 | molecular_function | heme binding |
| N | 0004601 | molecular_function | peroxidase activity |
| N | 0006979 | biological_process | response to oxidative stress |
| N | 0020037 | molecular_function | heme binding |
| O | 0004601 | molecular_function | peroxidase activity |
| O | 0006979 | biological_process | response to oxidative stress |
| O | 0020037 | molecular_function | heme binding |
| P | 0004601 | molecular_function | peroxidase activity |
| P | 0006979 | biological_process | response to oxidative stress |
| P | 0020037 | molecular_function | heme binding |
| S | 0004601 | molecular_function | peroxidase activity |
| S | 0006979 | biological_process | response to oxidative stress |
| S | 0020037 | molecular_function | heme binding |
| T | 0004601 | molecular_function | peroxidase activity |
| T | 0006979 | biological_process | response to oxidative stress |
| T | 0020037 | molecular_function | heme binding |
| U | 0004601 | molecular_function | peroxidase activity |
| U | 0006979 | biological_process | response to oxidative stress |
| U | 0020037 | molecular_function | heme binding |
| V | 0004601 | molecular_function | peroxidase activity |
| V | 0006979 | biological_process | response to oxidative stress |
| V | 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 | GLU408-LEU418 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 32 |
| 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 | THR334 | |
| H | PHE336 | |
| H | ASP338 | |
| H | SER340 | |
| J | THR334 | |
| J | PHE336 | |
| J | ASP338 | |
| J | SER340 | |
| N | THR334 | |
| N | PHE336 | |
| N | ASP338 | |
| B | PHE336 | |
| N | SER340 | |
| P | THR334 | |
| P | PHE336 | |
| P | ASP338 | |
| P | SER340 | |
| T | THR334 | |
| T | PHE336 | |
| T | ASP338 | |
| T | SER340 | |
| V | THR334 | |
| B | ASP338 | |
| V | PHE336 | |
| V | ASP338 | |
| V | SER340 | |
| B | SER340 | |
| D | THR334 | |
| D | PHE336 | |
| D | ASP338 | |
| D | SER340 | |
| H | THR334 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | BINDING: covalent => ECO:0000269|PubMed:23843990, ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, ECO:0007744|PDB:4EJX |
| Chain | Residue | Details |
| B | GLU408 | |
| N | MET409 | |
| P | GLU408 | |
| P | MET409 | |
| T | GLU408 | |
| T | MET409 | |
| V | GLU408 | |
| V | MET409 | |
| B | MET409 | |
| D | GLU408 | |
| D | MET409 | |
| H | GLU408 | |
| H | MET409 | |
| J | GLU408 | |
| J | MET409 | |
| N | GLU408 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| 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 | HIS502 | |
| D | HIS502 | |
| H | HIS502 | |
| J | HIS502 | |
| N | HIS502 | |
| P | HIS502 | |
| T | HIS502 | |
| V | HIS502 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | SITE: Transition state stabilizer |
| Chain | Residue | Details |
| B | ARG405 | |
| D | ARG405 | |
| H | ARG405 | |
| J | ARG405 | |
| N | ARG405 | |
| P | ARG405 | |
| T | ARG405 | |
| V | ARG405 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | MOD_RES: Cysteine sulfenic acid (-SOH) => ECO:0000269|PubMed:7840679 |
| Chain | Residue | Details |
| B | CSO316 | |
| D | CSO316 | |
| H | CSO316 | |
| J | CSO316 | |
| N | CSO316 | |
| P | CSO316 | |
| T | CSO316 | |
| V | CSO316 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:20332087 |
| Chain | Residue | Details |
| B | ASN323 | |
| D | ASN323 | |
| H | ASN323 | |
| J | ASN323 | |
| N | ASN323 | |
| P | ASN323 | |
| T | ASN323 | |
| V | ASN323 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 16 |
| 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 | ASN355 | |
| N | ASN391 | |
| P | ASN355 | |
| P | ASN391 | |
| T | ASN355 | |
| T | ASN391 | |
| V | ASN355 | |
| V | ASN391 | |
| B | ASN391 | |
| D | ASN355 | |
| D | ASN391 | |
| H | ASN355 | |
| H | ASN391 | |
| J | ASN355 | |
| J | ASN391 | |
| N | ASN355 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 8 |
| 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 | ASN483 | |
| D | ASN483 | |
| H | ASN483 | |
| J | ASN483 | |
| N | ASN483 | |
| P | ASN483 | |
| T | ASN483 | |
| V | ASN483 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 8 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:20332087 |
| Chain | Residue | Details |
| B | ASN729 | |
| D | ASN729 | |
| H | ASN729 | |
| J | ASN729 | |
| N | ASN729 | |
| P | ASN729 | |
| T | ASN729 | |
| V | ASN729 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 1 |
| Details | M-CSA 601 |
| Chain | Residue | Details |
| B | ARG405 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 1 |
| Details | M-CSA 601 |
| Chain | Residue | Details |
| D | ARG405 | electrostatic stabiliser |
| site_id | MCSA3 |
| Number of Residues | 1 |
| Details | M-CSA 601 |
| Chain | Residue | Details |
| H | ARG405 | electrostatic stabiliser |
| site_id | MCSA4 |
| Number of Residues | 1 |
| Details | M-CSA 601 |
| Chain | Residue | Details |
| J | ARG405 | electrostatic stabiliser |
| site_id | MCSA5 |
| Number of Residues | 1 |
| Details | M-CSA 601 |
| Chain | Residue | Details |
| N | ARG405 | electrostatic stabiliser |
| site_id | MCSA6 |
| Number of Residues | 1 |
| Details | M-CSA 601 |
| Chain | Residue | Details |
| P | ARG405 | electrostatic stabiliser |
| site_id | MCSA7 |
| Number of Residues | 1 |
| Details | M-CSA 601 |
| Chain | Residue | Details |
| T | ARG405 | electrostatic stabiliser |
| site_id | MCSA8 |
| Number of Residues | 1 |
| Details | M-CSA 601 |
| Chain | Residue | Details |
| V | ARG405 | electrostatic stabiliser |
