Structure of PDB 3fsj Chain X

Receptor sequence
>3fsjX (length=524) Species: 303 (Pseudomonas putida) [Search protein sequence]
ASVHGTTYELLRRQGIDTVFGNPGSNELPFLKDFPEDFRYILALQEACVV
GIADGYAQASRKPAFINLHSAAGTGNAMGALSNAWNSHSPLIVTAGQQTR
AMIGVEALLTNVDAANLPRPLVKWSYEPASAAEVPHAMSRAIHMASMAPQ
GPVYLSVPYDDWDKDADPQSHHLFDRHVSSSVRLNDQDLDILVKALNSAS
NPAIVLGPDVDAANANADCVMLAERLKAPVWVAPSAPRCPFPTRHPCFRG
LMPAGIAAISQLLEGHDVVLVIGAPVFRYHQYDPGQYLKPGTRLISVTCD
PLEAARAPMGDAIVADIGAMASALANLVEESSRQLPTAAPEPAKVDQDAG
RLHPETVFDTLNDMAPENAIYLNESTSTTAQMWQRLNMRNPGSYYFCAAG
GLGFALPAAIGVQLAEPERQVIAVIGDGSANYSISALWTAAQYNIPTIFV
IMNNGTYGALRWFAGVLEAENVPGLDVPGIDFRALAKGYGVQALKADNLE
QLKGSLQEALSAKGPVLIEVSTVS
3D structure
PDB3fsj Snapshot of a reaction intermediate: analysis of benzoylformate decarboxylase in complex with a benzoylphosphonate inhibitor.
ChainX
Resolution1.37 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G25 S26 E28 E47 H70 L109 L110 T111 N112 H281 G401 D428 N455 T457 Y458 A460 L461 S525
Catalytic site (residue number reindexed from 1) G24 S25 E27 E46 H69 L108 L109 T110 N111 H280 G400 D427 N454 T456 Y457 A459 L460 S524
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 D7K X H281 T377 S378 F397 G401 L403 G427 D428 G429 S430 Y433 T457 Y458 G459 A460 L461 F464 V524 S525 H280 T376 S377 F396 G400 L402 G426 D427 G428 S429 Y432 T456 Y457 G458 A459 L460 F463 V523 S524 MOAD: Kd=0.113mM
PDBbind-CN: -logKd/Ki=3.95,Kd=0.113mM
BS02 CA X D428 N455 T457 D427 N454 T456
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:3fsj, PDBe:3fsj, PDBj:3fsj
PDBsum3fsj
PubMed19320438
UniProtP20906|MDLC_PSEPU Benzoylformate decarboxylase (Gene Name=mdlC)

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