5AHK
Crystal structure of acetohydroxy acid synthase Pf5 from Pseudomonas protegens
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0003824 | molecular_function | catalytic activity |
A | 0003984 | molecular_function | acetolactate synthase activity |
A | 0005948 | cellular_component | acetolactate synthase complex |
A | 0009097 | biological_process | isoleucine biosynthetic process |
A | 0009099 | biological_process | L-valine biosynthetic process |
A | 0019752 | biological_process | carboxylic acid metabolic process |
A | 0030976 | molecular_function | thiamine pyrophosphate binding |
A | 0046872 | molecular_function | metal ion binding |
A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
B | 0000166 | molecular_function | nucleotide binding |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0003824 | molecular_function | catalytic activity |
B | 0003984 | molecular_function | acetolactate synthase activity |
B | 0005948 | cellular_component | acetolactate synthase complex |
B | 0009097 | biological_process | isoleucine biosynthetic process |
B | 0009099 | biological_process | L-valine biosynthetic process |
B | 0019752 | biological_process | carboxylic acid metabolic process |
B | 0030976 | molecular_function | thiamine pyrophosphate binding |
B | 0046872 | molecular_function | metal ion binding |
B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE TPP A 700 |
Chain | Residue |
A | VAL394 |
A | GLY448 |
A | ASN473 |
A | SER475 |
A | LEU476 |
A | GLY477 |
A | MET478 |
A | VAL479 |
A | MG702 |
A | HOH2339 |
A | HOH2353 |
A | GLY395 |
B | LEU22 |
B | ILE23 |
B | GLU48 |
B | PRO76 |
B | ASN80 |
B | GLN119 |
A | ASN396 |
A | ASN397 |
A | GLY420 |
A | MET422 |
A | GLY445 |
A | ASP446 |
A | GLY447 |
site_id | AC2 |
Number of Residues | 37 |
Details | BINDING SITE FOR RESIDUE FAD A 701 |
Chain | Residue |
A | ARG158 |
A | GLY218 |
A | GLY219 |
A | GLY220 |
A | SER224 |
A | SER244 |
A | LEU245 |
A | LYS246 |
A | MET260 |
A | LEU261 |
A | ALA263 |
A | TYR264 |
A | GLY283 |
A | SER284 |
A | ARG285 |
A | ASP287 |
A | ARG289 |
A | GLN290 |
A | ASP308 |
A | LEU309 |
A | GLN310 |
A | GLN313 |
A | ILE326 |
A | GLU327 |
A | LEU328 |
A | GLN398 |
A | MET399 |
A | SER416 |
A | GLY417 |
A | GLY418 |
A | HOH2089 |
A | HOH2091 |
A | HOH2092 |
A | HOH2205 |
A | HOH2254 |
A | HOH2418 |
B | PHE118 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 702 |
Chain | Residue |
A | ASP446 |
A | ASN473 |
A | SER475 |
A | TPP700 |
A | HOH2353 |
site_id | AC4 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE TPP B 700 |
Chain | Residue |
A | LEU22 |
A | ILE23 |
A | GLU48 |
A | PRO76 |
A | ASN80 |
A | GLN119 |
B | VAL394 |
B | GLY395 |
B | ASN396 |
B | ASN397 |
B | GLY420 |
B | MET422 |
B | GLY445 |
B | ASP446 |
B | GLY447 |
B | GLY448 |
B | ASN473 |
B | SER475 |
B | LEU476 |
B | GLY477 |
B | MET478 |
B | MG702 |
B | HOH2375 |
B | HOH2391 |
site_id | AC5 |
Number of Residues | 37 |
Details | BINDING SITE FOR RESIDUE FAD B 701 |
Chain | Residue |
B | LYS246 |
B | MET260 |
B | LEU261 |
B | ALA263 |
B | TYR264 |
B | GLY283 |
B | SER284 |
B | ARG285 |
B | ASP287 |
B | ARG289 |
B | GLN290 |
B | ASP308 |
B | LEU309 |
B | GLN310 |
B | GLN313 |
B | ILE326 |
B | GLU327 |
B | LEU328 |
B | GLN398 |
B | MET399 |
B | GLY417 |
B | GLY418 |
B | MET478 |
B | HOH2068 |
B | HOH2069 |
B | HOH2070 |
B | HOH2203 |
B | HOH2272 |
B | HOH2466 |
A | PHE118 |
B | ARG158 |
B | GLY218 |
B | GLY219 |
B | GLY220 |
B | SER224 |
B | SER244 |
B | LEU245 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 702 |
Chain | Residue |
B | ASP446 |
B | ASN473 |
B | SER475 |
B | TPP700 |
B | HOH2391 |