4GG1
Crystal Structure of Benzoylformate Decarboxylase Mutant L403T
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 | 0009056 | biological_process | catabolic process |
A | 0016831 | molecular_function | carboxy-lyase activity |
A | 0018924 | biological_process | mandelate metabolic 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 | 26 |
Details | BINDING SITE FOR RESIDUE TZD A 601 |
Chain | Residue |
A | ASN23 |
A | SER378 |
A | GLY401 |
A | GLY402 |
A | THR403 |
A | GLY427 |
A | ASP428 |
A | GLY429 |
A | SER430 |
A | TYR433 |
A | ASN455 |
A | PRO24 |
A | THR457 |
A | TYR458 |
A | GLY459 |
A | ALA460 |
A | CA602 |
A | HOH705 |
A | HOH790 |
A | GLY25 |
A | GLU47 |
A | HIS70 |
A | ASN77 |
A | GLU375 |
A | SER376 |
A | THR377 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA A 602 |
Chain | Residue |
A | ASP428 |
A | ASN455 |
A | THR457 |
A | TZD601 |
A | HOH716 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE CA A 603 |
Chain | Residue |
A | GLU37 |
A | ASP364 |
A | HOH765 |
A | HOH906 |
A | HOH1016 |
A | HOH1017 |
A | HOH1038 |
A | HOH1257 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA A 604 |
Chain | Residue |
A | ASN117 |
A | ASN117 |
A | LEU118 |
A | LEU118 |
A | ARG120 |
A | ARG120 |
site_id | AC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL A 605 |
Chain | Residue |
A | LEU43 |
A | GLN443 |
A | TYR444 |
A | GLY475 |
A | LEU476 |
A | ASP477 |
A | HOH1055 |
A | HOH1086 |
A | HOH1197 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 606 |
Chain | Residue |
A | ALA196 |
A | ARG294 |
A | ILE296 |
A | ASP312 |
A | HOH805 |
A | HOH1088 |
Functional Information from PROSITE/UniProt
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 | 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 | HIS281 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | GLY401 | electrostatic stabiliser, hydrogen bond acceptor |