Structure of PDB 3fzn Chain D

Receptor sequence

>3fznD (length=523) Species: 303 (Pseudomonas putida) [Search protein sequence]

ASVHGTTYELLRRQGIDTVFGNPGSNELPFLKDFPEDFRYILALQEACVV
GIADGYAQASRKPAFINLHSAAGTGNAMGALSNAWNSHSPLIVTAGQQTR
AMIGVEALLTNVDAANLPRPLVKWSYEPASAAEVPHAMSRAIHMASMAPQ
GPVYLSVPYDDWDKDADPQSHHLFDRHVSSSVRLNDQDLDILVKALNSAS
NPAIVLGPDVDAANANADCVMLAERLKAPVWVAPSAPRCPFPTRHPCFRG
LMPAGIAAISQLLEGHDVVLVIGAPVFRYHQYDPGQYLKPGTRLISVTCD
PLEAARAPMGDAIVADIGAMASALANLVEESSRQLPTAAPEPAKVDQDAG
RLHPETVFDTLNDMAPENAIYLNESTSTTAQMWQRLNMRNPGSYYFCAAG
GLGFALPAAIGVQLAEPERQVIAVIGDGSANYSISALWTAAQYNIPTIFV
IMNNGTYGALRWFAGVLEAENVPGLDVPGIDFRALAKGYGVQALKADNLE
QLKGSLQEALSAKGPVLIEVSTV

3D structure

PDB

3fzn Structural and kinetic studies on native intermediates and an intermediate analogue in benzoylformate decarboxylase reveal a least motion mechanism with an unprecedented short-lived predecarboxylation intermediate.

Chain

Resolution

1.62 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 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)
BS01	PO4	D	Q170 H172	Q169 H171
BS02	D7K	D	N23 P24 G25 S26 E47 H70	N22 P23 G24 S25 E46 H69
BS03	D7K	D	H281 T377 S378 G401 L403 G427 G429 S430 Y433 N455 T457 Y458 G459 A460 L461 F464	H280 T376 S377 G400 L402 G426 G428 S429 Y432 N454 T456 Y457 G458 A459 L460 F463
BS04	MG	D	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

View graph for
Molecular Function

View graph for
Biological Process

External links

PDB	RCSB:3fzn, PDBe:3fzn, PDBj:3fzn
PDBsum	3fzn
PubMed	19182954
UniProt	P20906\|MDLC_PSEPU Benzoylformate decarboxylase (Gene Name=mdlC)

[Back to BioLiP]