2PGO
The crystal structure of FAD and ThDP dependent Cyclohexane-1,2-dione Hydrolase (Cdh) from Azoarcus sp. strain 22Lin
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 0016787 | molecular_function | hydrolase activity |
| 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 | 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 | 0016787 | molecular_function | hydrolase activity |
| 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 | 3 |
| Details | BINDING SITE FOR RESIDUE PO4 B 625 |
| Chain | Residue |
| B | GLN388 |
| B | ILE410 |
| B | GLN412 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 608 |
| Chain | Residue |
| A | ASP451 |
| A | ASN478 |
| A | SER480 |
| A | HOH711 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 610 |
| Chain | Residue |
| B | GLN116 |
| B | HIS28 |
| B | HIS76 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 609 |
| Chain | Residue |
| B | ASP451 |
| B | ASN478 |
| B | SER480 |
| B | HOH721 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 611 |
| Chain | Residue |
| A | HIS28 |
| A | HIS76 |
| A | GLN116 |
| site_id | AC6 |
| Number of Residues | 38 |
| Details | BINDING SITE FOR RESIDUE FAD A 612 |
| Chain | Residue |
| A | ARG94 |
| A | HIS153 |
| A | GLY213 |
| A | GLY214 |
| A | GLY215 |
| A | ARG218 |
| A | SER219 |
| A | THR239 |
| A | SER240 |
| A | THR241 |
| A | ALA257 |
| A | GLY258 |
| A | PHE259 |
| A | CYS260 |
| A | GLY261 |
| A | GLY279 |
| A | SER280 |
| A | ARG281 |
| A | SER283 |
| A | TRP285 |
| A | GLY286 |
| A | ASP302 |
| A | THR303 |
| A | ASP304 |
| A | ALA320 |
| A | ASP321 |
| A | ALA322 |
| A | SER420 |
| A | MET421 |
| A | ALA422 |
| A | GLY424 |
| A | HOH644 |
| A | HOH657 |
| A | HOH664 |
| A | HOH686 |
| A | HOH687 |
| A | HOH818 |
| A | HOH819 |
| site_id | AC7 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE TPP A 614 |
| Chain | Residue |
| A | ILE398 |
| A | GLY399 |
| A | ASN400 |
| A | HIS401 |
| A | GLY424 |
| A | LEU426 |
| A | GLY450 |
| A | ASP451 |
| A | GLY452 |
| A | ALA453 |
| A | TYR456 |
| A | ASN478 |
| A | SER480 |
| A | TYR481 |
| A | GLY482 |
| A | ALA483 |
| A | ASN484 |
| A | HOH692 |
| A | HOH711 |
| B | ILE26 |
| B | GLU52 |
| B | HIS76 |
| site_id | AC8 |
| Number of Residues | 38 |
| Details | BINDING SITE FOR RESIDUE FAD B 613 |
| Chain | Residue |
| B | THR303 |
| B | ASP304 |
| B | ALA320 |
| B | ASP321 |
| B | ALA322 |
| B | SER420 |
| B | MET421 |
| B | ALA422 |
| B | GLY424 |
| B | HOH633 |
| B | HOH647 |
| B | HOH656 |
| B | HOH677 |
| B | HOH727 |
| B | HOH857 |
| B | HOH896 |
| B | HIS153 |
| B | GLY213 |
| B | GLY214 |
| B | GLY215 |
| B | ARG218 |
| B | SER219 |
| B | THR239 |
| B | SER240 |
| B | THR241 |
| B | ALA257 |
| B | GLY258 |
| B | PHE259 |
| B | CYS260 |
| B | GLY261 |
| B | GLY279 |
| B | SER280 |
| B | ARG281 |
| B | LEU282 |
| B | SER283 |
| B | TRP285 |
| B | GLY286 |
| B | ASP302 |
| site_id | AC9 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE TPP B 615 |
| Chain | Residue |
| A | ILE26 |
| A | GLU52 |
| A | HIS76 |
| A | HOH1148 |
| B | ILE398 |
| B | GLY399 |
| B | ASN400 |
| B | HIS401 |
| B | GLY424 |
| B | LEU426 |
| B | GLY450 |
| B | ASP451 |
| B | GLY452 |
| B | ALA453 |
| B | TYR456 |
| B | ASN478 |
| B | SER480 |
| B | TYR481 |
| B | GLY482 |
| B | ALA483 |
| B | ASN484 |
| B | HOH645 |
| B | HOH721 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MPD A 620 |
| Chain | Residue |
| A | GLY399 |
| A | LEU487 |
| A | LEU551 |
| A | LEU563 |
| A | HOH696 |
| B | HIS28 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD A 621 |
| Chain | Residue |
| A | THR249 |
| A | GLN388 |
| A | ILE410 |
| A | GLN412 |
