4JUD
Crystal Structure of the Ser26Thr mutant of Benzoylformate Decarboxylase from Pseudomonas putida
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| X | 0000287 | molecular_function | magnesium ion binding |
| X | 0003824 | molecular_function | catalytic activity |
| X | 0009056 | biological_process | catabolic process |
| X | 0016831 | molecular_function | carboxy-lyase activity |
| X | 0018924 | biological_process | mandelate metabolic process |
| X | 0019596 | biological_process | mandelate catabolic process |
| X | 0019752 | biological_process | carboxylic acid metabolic process |
| X | 0030976 | molecular_function | thiamine pyrophosphate binding |
| X | 0046872 | molecular_function | metal ion binding |
| X | 0050695 | molecular_function | benzoylformate decarboxylase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE TZD X 601 |
| Chain | Residue |
| X | ASN23 |
| X | GLY401 |
| X | LEU403 |
| X | GLY427 |
| X | ASP428 |
| X | GLY429 |
| X | SER430 |
| X | TYR433 |
| X | THR457 |
| X | TYR458 |
| X | GLY459 |
| X | PRO24 |
| X | ALA460 |
| X | CA603 |
| X | GOL605 |
| X | HOH714 |
| X | HOH779 |
| X | GLY25 |
| X | GLU47 |
| X | HIS70 |
| X | ASN77 |
| X | GLU375 |
| X | THR377 |
| X | SER378 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG X 602 |
| Chain | Residue |
| X | ASN117 |
| X | ASN117 |
| X | LEU118 |
| X | LEU118 |
| X | ARG120 |
| X | ARG120 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA X 603 |
| Chain | Residue |
| X | ASP428 |
| X | ASN455 |
| X | THR457 |
| X | TZD601 |
| X | HOH704 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL X 604 |
| Chain | Residue |
| X | ARG13 |
| X | ASP38 |
| X | LYS504 |
| X | HOH866 |
| X | HOH944 |
| X | HOH1006 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL X 605 |
| Chain | Residue |
| X | HIS281 |
| X | THR377 |
| X | GLY401 |
| X | TZD601 |
| X | HOH927 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL X 606 |
| Chain | Residue |
| X | TRP86 |
| X | GLU107 |
| X | ARG279 |
| X | ASP301 |
| X | LEU303 |
| X | GLU304 |
| X | ARG307 |
| X | HOH916 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL X 607 |
| Chain | Residue |
| X | ALA196 |
| X | ARG294 |
| X | ASP312 |
| X | HOH979 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL X 608 |
| Chain | Residue |
| X | ALA102 |
| X | GLY105 |
| X | GLU134 |
| X | HIS137 |
| X | ASP168 |
| X | TYR288 |
| X | HOH784 |
| X | HOH805 |
| X | HOH967 |
Functional Information from PROSITE/UniProt
| site_id | PS00187 |
| Number of Residues | 20 |
| Details | TPP_ENZYMES Thiamine pyrophosphate enzymes signature. IGvqlaePerqvIaViGDGS |
| Chain | Residue | Details |
| X | ILE411-SER430 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | BINDING: |
| Chain | Residue | Details |
| X | ASN117 | |
| X | LEU118 | |
| X | ARG120 | |
| X | ASP428 | |
| X | ASN455 | |
| X | THR457 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 220 |
| Chain | Residue | Details |
| X | GLY25 | electrostatic stabiliser, hydrogen bond donor |
| X | THR26 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| X | GLU28 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| X | GLU47 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| X | HIS70 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| X | HIS281 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| X | GLY401 | electrostatic stabiliser, hydrogen bond acceptor |
