Structure of PDB 4mzx Chain A

Receptor sequence

>4mzxA (length=525) Species: 303 (Pseudomonas putida) [Search protein sequence]

ASVHGTTYELLRRQGIDTVFGNPGSNELPFLKDFPEDFRYILALQEACVV
GIADGYAQASRKPAFINLHSAAGTGNAMGALSNAWNSHSPLIVTAGQQTR
AMIGVEALLTNVDAANLPRPLVKWSYEPASAAEVPHAMSRAIHMASMAPQ
GPVYLSVPYDDWDKDADPQSHHLFDRHVSSSVRLNDQDLDILVKALNSAS
NPAIVLGPDVDAANANADCVMLAERLKAPVWVAPSAPRCPFPTRHPCFRG
LMPAGIAAISQLLEGHDVVLVIGAPVFRYHQYDPGQYLKPGTRLISVTCD
PLEAARAPMGDAIVADIGAMASALANLVEESSRQLPTAAPEPAKVDQDAG
RLHPETVFDTLNDMAPENAIYLNESLSTTAQMWQRLNMRNPGSYYFCAAG
GLGFALPAAIGVQLAEPERQVIAVIGDGSANYSISALWTAAQYNIPTIFV
IMNNGTYGYLRWFAGVLEAENVPGLDVPGIDFRALAKGYGVQALKADNLE
QLKGSLQEALSAKGPVLIEVSTVSP

3D structure

PDB

4mzx Mechanistic and structural insight to an evolved benzoylformate decarboxylase with enhanced activity towards pyruvate

Chain

Resolution

1.558 Å

3D
structure

Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]

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 Y460 L461 F464 S525
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 Y459 L460 F463 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	CA	A	D428 N455 T457	D427 N454 T456
BS02	TZD	A	L377 S378 G401 L403 G427 D428 G429 S430 Y433 T457 Y458 G459 Y460 L461	L376 S377 G400 L402 G426 D427 G428 S429 Y432 T456 Y457 G458 Y459 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

View graph for
Molecular Function

View graph for
Biological Process

External links

PDB	RCSB:4mzx, PDBe:4mzx, PDBj:4mzx
PDBsum	4mzx
PubMed
UniProt	P20906\|MDLC_PSEPU Benzoylformate decarboxylase (Gene Name=mdlC)

[Back to BioLiP]