6M2Y
Crystal structure of a formolase, BFD variant M6 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 | 20 |
Details | binding site for residue TPP A 601 |
Chain | Residue |
A | ASN23 |
A | GLY429 |
A | SER430 |
A | TYR433 |
A | ASN455 |
A | THR457 |
A | TYR458 |
A | GLY459 |
A | MET460 |
A | MG602 |
A | HOH733 |
A | PRO24 |
A | HOH819 |
A | GLU47 |
A | THR377 |
A | SER378 |
A | GLY401 |
A | LEU403 |
A | GLY427 |
A | ASP428 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue MG A 602 |
Chain | Residue |
A | ASP428 |
A | ASN455 |
A | THR457 |
A | TPP601 |
A | HOH819 |
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 | PHE26 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
A | GLU28 | 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 | TYR281 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | GLY401 | electrostatic stabiliser, hydrogen bond acceptor |