Structure of PDB 2v3w Chain D Binding Site BS01

Receptor Information

>2v3w Chain D (length=526) Species: 303 (Pseudomonas putida) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

ASVHGTTYELLRRQGIDTVFGNPGSNELPFLKDFPEDFRYILALQEACVV
GIADGYAQASRKPAFINLHSAAGTGNAMGALSNAWNSHSPLIVTAGQQTR
AMIGVEALLTNVDAANLPRPLVKWSYEPASAAEVPHAMSRAIHMASMAPQ
GPVYLSVPYDDWDKDADPQSHHLFDRHVSSSVRLNDQDLDILVKALNSAS
NPAIVLGPDVDAANANADCVMLAERLKAPVWVAPSAPRCPFPTRHPCFRG
LMPAGIAAISQLLEGHDVVLVIGAPVFRYHQYDPGQYLKPGTRLISVTCD
PLEAARAPMGDAIVADIGAMASALANLVEESSRQLPTAAPEPAKVDQDAG
RLHPETVFDTLNDMAPENAIYLNESTSTTAQMWQRLNMRNPGSYYFCAAG
GLGFALPAAIGVQLAEPERQVIAVIGDGSANYSISALWTAAQYNIPTIFV
IMNNGTYGAARWFAGVLEAENVPGLDVPGIDFRALAKGYGVQALKADNLE
QLKGSLQEALSAKGPVLIEVSTVSPV

Ligand information

Ligand ID

InChI

InChI=1S/Mg/q+2

InChIKey

JLVVSXFLKOJNIY-UHFFFAOYSA-N

SMILES

Software	SMILES
ACDLabs 10.04 OpenEye OEToolkits 1.5.0	[Mg+2]
CACTVS 3.341	[Mg++]

Formula

Name

MAGNESIUM ION

PDB chain

2v3w Chain B Residue 1529 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

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Structure summary

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PDB	2v3w Rational Protein Design of Thdp-Dependent Enzymes-Engineering Stereoselectivity.
Resolution	2.2 Å
Binding residue (original residue number in PDB)	N117 L118 R120
Binding residue (residue number reindexed from 1)	N116 L117 R119
Annotation score	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 A461 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 A460 F463 S524
Enzyme Commision number	4.1.1.7: benzoylformate decarboxylase.

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

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Biological Process

External links

PDB	RCSB:2v3w, PDBe:2v3w, PDBj:2v3w
PDBsum	2v3w
PubMed	18224647
UniProt	P20906\|MDLC_PSEPU Benzoylformate decarboxylase (Gene Name=mdlC)

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