3D7K
Crystal structure of benzaldehyde lyase in complex with the inhibitor MBP
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 | valine biosynthetic process |
| A | 0016829 | molecular_function | lyase 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 | valine biosynthetic process |
| B | 0016829 | molecular_function | lyase 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 | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 571 |
| Chain | Residue |
| A | ASP448 |
| A | ASN475 |
| A | SER477 |
| A | D7K572 |
| A | HOH596 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 571 |
| Chain | Residue |
| B | HOH618 |
| B | ASP448 |
| B | ASN475 |
| B | SER477 |
| B | D7K572 |
| site_id | AC3 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE D7K A 572 |
| Chain | Residue |
| A | GLY393 |
| A | ALA394 |
| A | LEU395 |
| A | THR396 |
| A | GLY419 |
| A | SER420 |
| A | MET421 |
| A | GLY447 |
| A | ASP448 |
| A | GLY449 |
| A | SER450 |
| A | TYR453 |
| A | ASN475 |
| A | SER477 |
| A | TRP478 |
| A | GLY479 |
| A | ALA480 |
| A | THR481 |
| A | CA571 |
| A | HOH596 |
| B | HIS26 |
| B | GLY27 |
| B | ALA28 |
| B | GLU50 |
| B | THR73 |
| B | ASN80 |
| B | GLN113 |
| B | HOH608 |
| site_id | AC4 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE D7K B 572 |
| Chain | Residue |
| A | HIS26 |
| A | GLY27 |
| A | ALA28 |
| A | GLU50 |
| A | THR73 |
| A | ASN80 |
| A | GLN113 |
| B | GLY393 |
| B | ALA394 |
| B | LEU395 |
| B | THR396 |
| B | TYR397 |
| B | GLY419 |
| B | SER420 |
| B | MET421 |
| B | GLY447 |
| B | ASP448 |
| B | GLY449 |
| B | SER450 |
| B | TYR453 |
| B | ASN475 |
| B | SER477 |
| B | TRP478 |
| B | GLY479 |
| B | ALA480 |
| B | THR481 |
| B | CA571 |
| B | HOH583 |
| B | HOH618 |
