Structure of PDB 1bfd Chain A

Receptor sequence
>1bfdA (length=523) Species: 303 (Pseudomonas putida) [Search protein sequence]
ASVHGTTYELLRRQGIDTVFGNPGSNELPFLKDFPEDFRYILALQEACVV
GIADGYAQASRKPAFINLHSAAGTGNAMGALSNAWNSHSPLIVTAGQQTR
AMIGVEALLTNVDAANLPRPLVKWSYEPASAAEVPHAMSRAIHMASMAPQ
GPVYLSVPYDDWDKDADPQSHHLFDRHVSSSVRLNDQDLDILVKALNSAS
NPAIVLGPDVDAANANADCVMLAERLKAPVWVAPSAPRCPFPTRHPCFRG
LMPAGIAAISQLLEGHDVVLVIGAPVFRYHQYDPGQYLKPGTRLISVTCD
PLEAARAPMGDAIVADIGAMASALANLVEESSRQLPTAAPEPAKVDQDAG
RLHPETVFDTLNDMAPENAIYLNESTSTTAQMWQRLNMRNPGSYYFCAAG
GLGFALPAAIGVQLAEPERQVIAVIGDGSANYSISALWTAAQYNIPTIFV
IMNNGTYGALRWFAGVLEAENVPGLDVPGIDFRALAKGYGVQALKADNLE
QLKGSLQEALSAKGPVLIEVSTV
3D structure
PDB1bfd The crystal structure of benzoylformate decarboxylase at 1.6 A resolution: diversity of catalytic residues in thiamin diphosphate-dependent enzymes.
ChainA
Resolution1.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N23 G25 S26 N27 E28 E47 H70 L109 L110 T111 N112 Y160 P254 H281 S376 G401 L403 D428 N455 T457 Y458 A460 L461 F464
Catalytic site (residue number reindexed from 1) N22 G24 S25 N26 E27 E46 H69 L108 L109 T110 N111 Y159 P253 H280 S375 G400 L402 D427 N454 T456 Y457 A459 L460 F463
Enzyme Commision number 4.1.1.7: benzoylformate decarboxylase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 CA A D428 N455 T457 D427 N454 T456
BS02 MG A N117 L118 R120 N116 L117 R119
BS03 TPP A T377 S378 L403 G427 D428 G429 S430 Y433 T457 Y458 G459 A460 L461 T376 S377 L402 G426 D427 G428 S429 Y432 T456 Y457 G458 A459 L460
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003824 catalytic activity
GO:0003984 acetolactate synthase activity
GO:0016831 carboxy-lyase activity
GO:0030976 thiamine pyrophosphate binding
GO:0046872 metal ion binding
GO:0050660 flavin adenine dinucleotide binding
GO:0050695 benzoylformate decarboxylase activity
Biological Process
GO:0009056 catabolic process
GO:0018924 mandelate metabolic process
GO:0019596 mandelate catabolic process
GO:0019752 carboxylic acid metabolic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1bfd, PDBe:1bfd, PDBj:1bfd
PDBsum1bfd
PubMed9665697
UniProtP20906|MDLC_PSEPU Benzoylformate decarboxylase (Gene Name=mdlC)

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