1PI3
E28Q mutant Benzoylformate Decarboxylase From Pseudomonas Putida
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 | 0016831 | molecular_function | carboxy-lyase activity |
| A | 0018924 | biological_process | mandelate metabolic process |
| A | 0019439 | biological_process | obsolete aromatic compound catabolic process |
| A | 0019596 | biological_process | mandelate catabolic 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 |
| A | 0050695 | molecular_function | benzoylformate decarboxylase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MG A 531 |
| Chain | Residue |
| A | ASN117 |
| A | ASN117 |
| A | LEU118 |
| A | LEU118 |
| A | ARG120 |
| A | ARG120 |
| A | HOH802 |
| A | HOH802 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 532 |
| Chain | Residue |
| A | ASN455 |
| A | THR457 |
| A | TZD530 |
| A | HOH936 |
| A | ASP428 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 533 |
| Chain | Residue |
| A | GLU37 |
| A | ASP364 |
| A | HOH690 |
| A | HOH699 |
| A | HOH728 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA A 534 |
| Chain | Residue |
| A | ASP347 |
| A | ALA416 |
| A | HOH697 |
| A | HOH700 |
| A | HOH711 |
| A | HOH860 |
| A | HOH883 |
| site_id | AC5 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE TZD A 530 |
| Chain | Residue |
| A | ASN23 |
| A | PRO24 |
| A | GLY25 |
| A | GLU47 |
| A | HIS70 |
| A | ASN77 |
| A | THR377 |
| A | SER378 |
| A | GLY401 |
| A | LEU403 |
| A | GLY427 |
| A | ASP428 |
| A | GLY429 |
| A | SER430 |
| A | TYR433 |
| A | ASN455 |
| A | THR457 |
| A | TYR458 |
| A | GLY459 |
| A | ALA460 |
| A | CA532 |
| A | HOH540 |
| A | HOH626 |
Functional Information from PROSITE/UniProt
| site_id | PS00187 |
| Number of Residues | 20 |
| Details | TPP_ENZYMES Thiamine pyrophosphate enzymes signature. IGvqlaePerqvIaViGDGS |
| Chain | Residue | Details |
| A | ILE411-SER430 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASN117 | |
| A | LEU118 | |
| A | ARG120 | |
| A | ASP428 | |
| A | ASN455 | |
| A | THR457 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 220 |
| Chain | Residue | Details |
| A | GLY25 | electrostatic stabiliser, hydrogen bond donor |
| A | SER26 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| A | GLN28 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | GLU47 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | HIS70 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | HIS281 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | GLY401 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bfd |
| Chain | Residue | Details |
| A | GLN28 | |
| A | HIS281 | |
| A | HIS70 |
