7LAG
CRYSTAL STRUCTURE OF MYELOPEROXIDASE SUBFORM C (MPO) COMPLEX WITH Compound-14 AKA 7-({1-[(3-phenoxyphenyl)methyl]-1H-pyrazol-4-yl}methyl)-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 | 4 |
Details | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
B | MET190 | |
E | MET190 | |
G | MET190 | |
I | MET190 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: covalent => ECO:0000269|PubMed:23843990, ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, ECO:0007744|PDB:4EJX |
Chain | Residue | Details |
B | ASN189 | |
I | ASN189 | |
I | THR337 | |
I | LEU338 | |
B | THR337 | |
B | LEU338 | |
E | ASN189 | |
E | THR337 | |
E | LEU338 | |
G | ASN189 | |
G | THR337 | |
G | LEU338 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: |
Chain | Residue | Details |
B | SER191 | |
E | SER191 | |
G | SER191 | |
I | SER191 |
site_id | SWS_FT_FI4 |
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 | GLU263 | |
G | LYS265 | |
G | LEU267 | |
G | PRO269 | |
I | GLU263 | |
I | LYS265 | |
I | LEU267 | |
I | PRO269 | |
B | LYS265 | |
B | LEU267 | |
B | PRO269 | |
E | GLU263 | |
E | LYS265 | |
E | LEU267 | |
E | PRO269 | |
G | GLU263 |
site_id | SWS_FT_FI5 |
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 | PRO431 | |
E | PRO431 | |
G | PRO431 | |
I | PRO431 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | SITE: Transition state stabilizer |
Chain | Residue | Details |
B | TYR334 | |
E | TYR334 | |
G | TYR334 | |
I | TYR334 |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | MOD_RES: Cysteine sulfenic acid (-SOH) => ECO:0000269|PubMed:7840679 |
Chain | Residue | Details |
B | GLU245 | |
E | GLU245 | |
G | GLU245 | |
I | GLU245 |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:20332087 |
Chain | Residue | Details |
B | LEU252 | |
E | LEU252 | |
G | LEU252 | |
I | LEU252 |
site_id | SWS_FT_FI9 |
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 | VAL284 | |
B | VAL320 | |
E | VAL284 | |
E | VAL320 | |
G | VAL284 | |
G | VAL320 | |
I | VAL284 | |
I | VAL320 |
site_id | SWS_FT_FI10 |
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 | ARG412 | |
E | ARG412 | |
G | ARG412 | |
I | ARG412 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 2 |
Details | M-CSA 601 |
Chain | Residue | Details |
B | MET190 | proton shuttle (general acid/base) |
B | TYR334 | electrostatic stabiliser |
site_id | MCSA2 |
Number of Residues | 2 |
Details | M-CSA 601 |
Chain | Residue | Details |
E | MET190 | proton shuttle (general acid/base) |
E | TYR334 | electrostatic stabiliser |
site_id | MCSA3 |
Number of Residues | 2 |
Details | M-CSA 601 |
Chain | Residue | Details |
G | MET190 | proton shuttle (general acid/base) |
G | TYR334 | electrostatic stabiliser |
site_id | MCSA4 |
Number of Residues | 2 |
Details | M-CSA 601 |
Chain | Residue | Details |
I | MET190 | proton shuttle (general acid/base) |
I | TYR334 | electrostatic stabiliser |