4DL1
Crystal Structure of human Myeloperoxidase with covalent thioxanthine analog
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 |
| E | 0004601 | molecular_function | peroxidase activity |
| E | 0006979 | biological_process | response to oxidative stress |
| E | 0020037 | molecular_function | heme binding |
| F | 0004601 | molecular_function | peroxidase activity |
| F | 0006979 | biological_process | response to oxidative stress |
| F | 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 |
| K | 0004601 | molecular_function | peroxidase activity |
| K | 0006979 | biological_process | response to oxidative stress |
| K | 0020037 | molecular_function | heme binding |
| L | 0004601 | molecular_function | peroxidase activity |
| L | 0006979 | biological_process | response to oxidative stress |
| L | 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 |
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 | 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 |
| C | THR168 | |
| G | PHE170 | |
| G | ASP172 | |
| G | SER174 | |
| H | THR168 | |
| H | PHE170 | |
| H | ASP172 | |
| H | SER174 | |
| K | THR168 | |
| K | PHE170 | |
| K | ASP172 | |
| C | PHE170 | |
| K | SER174 | |
| L | THR168 | |
| L | PHE170 | |
| L | ASP172 | |
| L | SER174 | |
| O | THR168 | |
| O | PHE170 | |
| O | ASP172 | |
| O | SER174 | |
| P | THR168 | |
| C | ASP172 | |
| P | PHE170 | |
| P | ASP172 | |
| P | SER174 | |
| C | SER174 | |
| D | THR168 | |
| D | PHE170 | |
| D | ASP172 | |
| D | SER174 | |
| G | THR168 |
| 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 |
| C | GLU242 | |
| K | MET243 | |
| L | GLU242 | |
| L | MET243 | |
| O | GLU242 | |
| O | MET243 | |
| P | GLU242 | |
| P | MET243 | |
| C | MET243 | |
| D | GLU242 | |
| D | MET243 | |
| G | GLU242 | |
| G | MET243 | |
| H | GLU242 | |
| H | MET243 | |
| K | GLU242 |
| 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 |
| C | HIS336 | |
| D | HIS336 | |
| G | HIS336 | |
| H | HIS336 | |
| K | HIS336 | |
| L | HIS336 | |
| O | HIS336 | |
| P | HIS336 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | SITE: Transition state stabilizer |
| Chain | Residue | Details |
| C | ARG239 | |
| D | ARG239 | |
| G | ARG239 | |
| H | ARG239 | |
| K | ARG239 | |
| L | ARG239 | |
| O | ARG239 | |
| P | ARG239 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | MOD_RES: Cysteine sulfenic acid (-SOH) => ECO:0000269|PubMed:7840679 |
| Chain | Residue | Details |
| C | CSO150 | |
| D | CSO150 | |
| G | CSO150 | |
| H | CSO150 | |
| K | CSO150 | |
| L | CSO150 | |
| O | CSO150 | |
| P | CSO150 |
| 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 |
| C | ASN157 | |
| D | ASN157 | |
| G | ASN157 | |
| H | ASN157 | |
| K | ASN157 | |
| L | ASN157 | |
| O | ASN157 | |
| P | ASN157 |
| 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 |
| C | ASN189 | |
| K | ASN225 | |
| L | ASN189 | |
| L | ASN225 | |
| O | ASN189 | |
| O | ASN225 | |
| P | ASN189 | |
| P | ASN225 | |
| C | ASN225 | |
| D | ASN189 | |
| D | ASN225 | |
| G | ASN189 | |
| G | ASN225 | |
| H | ASN189 | |
| H | ASN225 | |
| K | ASN189 |
| 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 |
| C | ASN317 | |
| D | ASN317 | |
| G | ASN317 | |
| H | ASN317 | |
| K | ASN317 | |
| L | ASN317 | |
| O | ASN317 | |
| P | ASN317 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 8 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:20332087 |
| Chain | Residue | Details |
| C | ASN563 | |
| D | ASN563 | |
| G | ASN563 | |
| H | ASN563 | |
| K | ASN563 | |
| L | ASN563 | |
| O | ASN563 | |
| P | ASN563 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 1 |
| Details | M-CSA 601 |
| Chain | Residue | Details |
| C | ARG239 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 1 |
| Details | M-CSA 601 |
| Chain | Residue | Details |
| D | ARG239 | electrostatic stabiliser |
| site_id | MCSA3 |
| Number of Residues | 1 |
| Details | M-CSA 601 |
| Chain | Residue | Details |
| G | ARG239 | electrostatic stabiliser |
| site_id | MCSA4 |
| Number of Residues | 1 |
| Details | M-CSA 601 |
| Chain | Residue | Details |
| H | ARG239 | electrostatic stabiliser |
| site_id | MCSA5 |
| Number of Residues | 1 |
| Details | M-CSA 601 |
| Chain | Residue | Details |
| K | ARG239 | electrostatic stabiliser |
| site_id | MCSA6 |
| Number of Residues | 1 |
| Details | M-CSA 601 |
| Chain | Residue | Details |
| L | ARG239 | electrostatic stabiliser |
| site_id | MCSA7 |
| Number of Residues | 1 |
| Details | M-CSA 601 |
| Chain | Residue | Details |
| O | ARG239 | electrostatic stabiliser |
| site_id | MCSA8 |
| Number of Residues | 1 |
| Details | M-CSA 601 |
| Chain | Residue | Details |
| P | ARG239 | electrostatic stabiliser |
