4GM1
Crystal Structure of Benzoylformate Decarboxylase Mutant L403S
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003824 | molecular_function | catalytic 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 | 0050695 | molecular_function | benzoylformate decarboxylase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 601 |
| Chain | Residue |
| A | ASP428 |
| A | ASN455 |
| A | THR457 |
| A | TZD606 |
| A | HOH724 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE CA A 602 |
| Chain | Residue |
| A | HOH1051 |
| A | HOH1072 |
| A | HOH1103 |
| A | HOH1118 |
| A | HOH1168 |
| A | GLU37 |
| A | ASP364 |
| A | HOH775 |
| A | HOH898 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 603 |
| Chain | Residue |
| A | ASN117 |
| A | ASN117 |
| A | LEU118 |
| A | LEU118 |
| A | ARG120 |
| A | ARG120 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 604 |
| Chain | Residue |
| A | ALA196 |
| A | ARG294 |
| A | ILE296 |
| A | ASP312 |
| A | HOH785 |
| A | HOH1126 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 605 |
| Chain | Residue |
| A | LEU43 |
| A | GLN443 |
| A | GLY475 |
| A | LEU476 |
| A | ASP477 |
| A | HOH1031 |
| A | HOH1128 |
| A | HOH1217 |
| site_id | AC6 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE TZD A 606 |
| Chain | Residue |
| A | ASN23 |
| A | PRO24 |
| A | GLY25 |
| A | GLU47 |
| A | HIS70 |
| A | ASN77 |
| A | GLU375 |
| A | THR377 |
| A | SER378 |
| A | GLY401 |
| A | GLY402 |
| A | SER403 |
| A | GLY427 |
| A | ASP428 |
| A | GLY429 |
| A | SER430 |
| A | TYR433 |
| A | ASN455 |
| A | THR457 |
| A | TYR458 |
| A | GLY459 |
| A | ALA460 |
| A | CA601 |
| A | HOH730 |
| A | HOH1226 |
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 |
