6WY0
CRYSTAL STRUCTURE OF MYELOPEROXIDASE SUBFORM C (MPO) COMPLEX WITH Compound-40 A.K.A 7-[(1R)-1-phenyl-3-{[(1r,4r)-4-phenylcyclohexyl]amino}propyl]-3H-[1,2,3]triazolo[4,5-b]pyridin-5-amine
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 |
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 |
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 | 16 |
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 | THR168 | |
G | PHE170 | |
G | ASP172 | |
G | SER174 | |
I | THR168 | |
I | PHE170 | |
I | ASP172 | |
I | SER174 | |
B | PHE170 | |
B | ASP172 | |
B | SER174 | |
E | THR168 | |
E | PHE170 | |
E | ASP172 | |
E | SER174 | |
G | THR168 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: covalent => ECO:0000269|PubMed:23843990, ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, ECO:0007744|PDB:4EJX |
Chain | Residue | Details |
B | GLU242 | |
B | MET243 | |
E | GLU242 | |
E | MET243 | |
G | GLU242 | |
G | MET243 | |
I | GLU242 | |
I | MET243 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
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 | HIS336 | |
E | HIS336 | |
G | HIS336 | |
I | HIS336 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | SITE: Transition state stabilizer |
Chain | Residue | Details |
B | ARG239 | |
E | ARG239 | |
G | ARG239 | |
I | ARG239 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | MOD_RES: Cysteine sulfenic acid (-SOH) => ECO:0000269|PubMed:7840679 |
Chain | Residue | Details |
B | CSO150 | |
E | CSO150 | |
G | CSO150 | |
I | CSO150 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:20332087 |
Chain | Residue | Details |
B | ASN157 | |
E | ASN157 | |
G | ASN157 | |
I | ASN157 |
site_id | SWS_FT_FI7 |
Number of Residues | 8 |
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 | ASN189 | |
B | ASN225 | |
E | ASN189 | |
E | ASN225 | |
G | ASN189 | |
G | ASN225 | |
I | ASN189 | |
I | ASN225 |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
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 | ASN317 | |
E | ASN317 | |
G | ASN317 | |
I | ASN317 |
site_id | SWS_FT_FI9 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:20332087 |
Chain | Residue | Details |
B | ASN563 | |
E | ASN563 | |
G | ASN563 | |
I | ASN563 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 1 |
Details | M-CSA 601 |
Chain | Residue | Details |
B | ARG239 | electrostatic stabiliser |
site_id | MCSA2 |
Number of Residues | 1 |
Details | M-CSA 601 |
Chain | Residue | Details |
E | 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 |
I | ARG239 | electrostatic stabiliser |