Structure of PDB 1mcz Chain E

Receptor sequence

>1mczE (length=524) Species: 303 (Pseudomonas putida) [Search protein sequence]

ASVHGTTYELLRRQGIDTVFGNPGSNELPFLKDFPEDFRYILALQEACVV
GIADGYAQASRKPAFINLHSAAGTGNAMGALSNAWNSHSPLIVTAGQQTR
AMIGVEALLTNVDAANLPRPLVKWSYEPASAAEVPHAMSRAIHMASMAPQ
GPVYLSVPYDDWDKDADPQSHHLFDRHVSSSVRLNDQDLDILVKALNSAS
NPAIVLGPDVDAANANADCVMLAERLKAPVWVAPSAPRCPFPTRHPCFRG
LMPAGIAAISQLLEGHDVVLVIGAPVFRYHQYDPGQYLKPGTRLISVTCD
PLEAARAPMGDAIVADIGAMASALANLVEESSRQLPTAAPEPAKVDQDAG
RLHPETVFDTLNDMAPENAIYLNESTSTTAQMWQRLNMRNPGSYYFCAAG
GLGFALPAAIGVQLAEPERQVIAVIGDGSANYSISALWTAAQYNIPTIFV
IMNNGTYGALRWFAGVLEAENVPGLDVPGIDFRALAKGYGVQALKADNLE
QLKGSLQEALSAKGPVLIEVSTVS

3D structure

PDB

1mcz Structural and Kinetic Analysis of Catalysis by a Thiamin Diphosphate-Dependent Enzyme, Benzoylformate Decarboxylase

Chain

Resolution

2.8 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 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 A459 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)
BS01	MG	E	D428 N455 T457	D427 N454 T456
BS02	TPP	E	T377 S378 G401 L403 G427 D428 G429 S430 Y433 Y458 G459 A460 L461	T376 S377 G400 L402 G426 D427 G428 S429 Y432 Y457 G458 A459 L460
BS03	RMN	E	H281 T377	H280 T376
BS04	TPP	E	N23 P24 E47 H70	N22 P23 E46 H69
BS05	RMN	E	S26 H70 L110	S25 H69 L109

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:1mcz, PDBe:1mcz, PDBj:1mcz
PDBsum	1mcz
PubMed	12590569
UniProt	P20906\|MDLC_PSEPU Benzoylformate decarboxylase (Gene Name=mdlC)

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