4K9L
Crystal Structure of the His281Thr mutant of 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 | 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 | 26 |
| Details | BINDING SITE FOR RESIDUE TZD A 601 |
| Chain | Residue |
| A | ASN23 |
| A | GLY401 |
| A | LEU403 |
| A | GLY427 |
| A | ASP428 |
| A | GLY429 |
| A | SER430 |
| A | TYR433 |
| A | ASN455 |
| A | THR457 |
| A | TYR458 |
| A | PRO24 |
| A | GLY459 |
| A | ALA460 |
| A | LEU461 |
| A | CA602 |
| A | EDO606 |
| A | HOH726 |
| A | HOH1134 |
| A | GLY25 |
| A | GLU47 |
| A | HIS70 |
| A | ASN77 |
| A | GLU375 |
| A | THR377 |
| A | SER378 |
| 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 | HOH714 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO A 603 |
| Chain | Residue |
| A | TRP86 |
| A | HIS89 |
| A | GLU107 |
| A | ASP301 |
| A | GLU304 |
| A | ARG307 |
| A | HOH858 |
| A | HOH1007 |
| A | HOH1084 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 604 |
| Chain | Residue |
| A | ALA149 |
| A | CYS300 |
| A | HOH850 |
| A | HOH850 |
| A | HOH948 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 605 |
| Chain | Residue |
| A | ASN215 |
| A | ALA216 |
| A | ASN217 |
| A | ALA218 |
| A | ASP219 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 606 |
| Chain | Residue |
| A | ASN77 |
| A | GLY80 |
| A | ASN84 |
| A | GLY402 |
| A | LEU403 |
| A | TZD601 |
| A | HOH720 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 607 |
| Chain | Residue |
| A | GLY256 |
| A | ILE257 |
| A | ALA258 |
| A | ALA259 |
| A | HOH1091 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO A 608 |
| Chain | Residue |
| A | PRO418 |
| A | GLU419 |
| A | ARG420 |
| A | GLN421 |
| A | HOH996 |
| A | HOH1001 |
| A | HOH1043 |
| A | HOH1132 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 609 |
| Chain | Residue |
| A | LYS496 |
| A | GLN502 |
| A | SER506 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 610 |
| Chain | Residue |
| A | ARG120 |
| A | TRP125 |
| A | SER126 |
| A | ARG141 |
| A | HOH854 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 611 |
| Chain | Residue |
| A | ALA2 |
| A | ASP166 |
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 | 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 | THR281 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | GLY401 | electrostatic stabiliser, hydrogen bond acceptor |
