5ETQ
S. aureus 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase complexed with AMPCPP and inhibitor at 1.96 angstrom resolution
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003848 | molecular_function | 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0009396 | biological_process | folic acid-containing compound biosynthetic process |
A | 0016301 | molecular_function | kinase activity |
A | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
A | 0046656 | biological_process | folic acid biosynthetic process |
A | 0046872 | molecular_function | metal ion binding |
B | 0003848 | molecular_function | 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0009396 | biological_process | folic acid-containing compound biosynthetic process |
B | 0016301 | molecular_function | kinase activity |
B | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
B | 0046656 | biological_process | folic acid biosynthetic process |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue MG A 201 |
Chain | Residue |
A | ASP95 |
A | ASP97 |
A | MG202 |
A | APC203 |
A | HOH342 |
A | HOH355 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue MG A 202 |
Chain | Residue |
A | APC203 |
A | HOH310 |
A | HOH327 |
A | ASP95 |
A | ASP97 |
A | MG201 |
site_id | AC3 |
Number of Residues | 24 |
Details | binding site for residue APC A 203 |
Chain | Residue |
A | LEU71 |
A | ARG83 |
A | ARG85 |
A | ARG92 |
A | ASP95 |
A | ASP97 |
A | ILE98 |
A | LYS110 |
A | LEU111 |
A | SER112 |
A | HIS115 |
A | ARG117 |
A | ARG121 |
A | MG201 |
A | MG202 |
A | YH2204 |
A | HOH301 |
A | HOH303 |
A | HOH310 |
A | HOH311 |
A | HOH327 |
A | HOH342 |
A | HOH348 |
A | HOH355 |
site_id | AC4 |
Number of Residues | 16 |
Details | binding site for residue YH2 A 204 |
Chain | Residue |
A | ASN11 |
A | THR43 |
A | ALA44 |
A | PRO45 |
A | VAL46 |
A | GLN51 |
A | PHE54 |
A | ASN56 |
A | GLY90 |
A | PRO91 |
A | ARG92 |
A | ARG121 |
A | PHE123 |
A | APC203 |
A | HOH342 |
A | HOH360 |
site_id | AC5 |
Number of Residues | 7 |
Details | binding site for residue NA A 205 |
Chain | Residue |
A | ASN27 |
A | TYR29 |
A | ILE32 |
A | HOH315 |
A | HOH370 |
B | NA205 |
B | HOH358 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue NA A 206 |
Chain | Residue |
A | ASP107 |
A | HOH333 |
B | ASP107 |
B | HOH311 |
B | HOH332 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue MG B 201 |
Chain | Residue |
B | ASP95 |
B | ASP97 |
B | MG202 |
B | APC203 |
B | HOH309 |
B | HOH341 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue MG B 202 |
Chain | Residue |
B | ASP95 |
B | ASP97 |
B | MG201 |
B | APC203 |
B | HOH329 |
B | HOH348 |
site_id | AC9 |
Number of Residues | 21 |
Details | binding site for residue APC B 203 |
Chain | Residue |
B | LEU71 |
B | ARG83 |
B | ARG92 |
B | ASP95 |
B | ASP97 |
B | ILE98 |
B | LYS110 |
B | LEU111 |
B | SER112 |
B | HIS115 |
B | ARG117 |
B | ARG121 |
B | MG201 |
B | MG202 |
B | HOH301 |
B | HOH309 |
B | HOH313 |
B | HOH329 |
B | HOH341 |
B | HOH348 |
B | HOH353 |
site_id | AD1 |
Number of Residues | 15 |
Details | binding site for residue YH2 B 204 |
Chain | Residue |
B | ALA44 |
B | PRO45 |
B | VAL46 |
B | GLN51 |
B | PHE54 |
B | ASN56 |
B | GLY90 |
B | PRO91 |
B | ARG92 |
B | ARG121 |
B | PHE123 |
B | HOH329 |
B | HOH347 |
B | ASN11 |
B | THR43 |
site_id | AD2 |
Number of Residues | 7 |
Details | binding site for residue NA B 205 |
Chain | Residue |
A | NA205 |
A | HOH315 |
A | HOH370 |
B | ASN27 |
B | TYR29 |
B | ILE32 |
B | HOH358 |
Functional Information from PROSITE/UniProt
site_id | PS00794 |
Number of Residues | 12 |
Details | HPPK 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase signature. RwGPRtlDVDIL |
Chain | Residue | Details |
A | ARG88-LEU99 |