Structure of PDB 5wdg Chain B Binding Site BS02

Receptor Information

>5wdg Chain B (length=554) Species: 573 (Klebsiella pneumoniae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

PRGSHMDKQYPVRQWAHGADLVVSQLEAQGVRQVFGIPGAKIDKVFDSLL
DSSIRIIPVRHEANAAFMAAAVGRITGKAGVALVTSGPGCSNLITGMATA
NSEGDPVVALGGAVKRADKAKQVHQSMDTVAMFSPVTKYAIEVTAPDALA
EVVSNAFRAAEQGRPGSAFVSLPQDVVDGPVSGKVLPASGAPQMGAAPDD
AIDQVAKLIAQAKNPIFLLGLMASQPENSKALRRLLETSHIPVTSTYQAA
GAVNQDNFSRFAGRVGLFNNQAGDRLLQLADLVICIGYSPVEYEPAMWNS
GNATLVHIDVLPAYEERNYTPDVELVGDIAGTLNKLAQNIDHRLVLSPQA
AEILRDRQHQRRGAQLNQFALHPLRIVRAMQDIVNSDVTLTVDMGSFHIW
IARYLYSFRARQVMISNGQQTMGVALPWAIGAWLVNPERKVVSVSGDGGF
LQSSMELETAVRLKANVLHLIWVDNGYNMVAIQEEKKYQRLSGVEFGPMD
FKAYAESFGAKGFAVESAEALEPTLRAAMDVDGPAVVAIPVDYRDNPLLM
GQLH

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

5wdg Chain B Residue 602 [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	5wdg Acetolactate Synthase from Klebsiella pneumoniae in Complex with Mechanism-Based Inhibitor
Resolution	2.12 Å
Binding residue (original residue number in PDB)	S129 T132
Binding residue (residue number reindexed from 1)	S134 T137
Annotation score	1

Enzymatic activity

Catalytic site (original residue number in PDB)	I32 G34 A35 K36 I37 E57 T80 H119 Q120 S121 Q169 L262 E289 M394 Q420 M422 D447 D474 G476 Y477 M479 V480 Q483 Y543
Catalytic site (residue number reindexed from 1)	I37 G39 A40 K41 I42 E62 T85 H124 Q125 S126 Q174 L267 E294 M394 Q420 M422 D447 D474 G476 Y477 M479 V480 Q483 Y543
Enzyme Commision number	2.2.1.6: acetolactate synthase.

Gene Ontology

	Molecular Function
GO:0000287	magnesium ion binding
GO:0003824	catalytic activity
GO:0003984	acetolactate synthase activity
GO:0016740	transferase activity
GO:0030976	thiamine pyrophosphate binding
GO:0046872	metal ion binding
GO:0050660	flavin adenine dinucleotide binding

	Biological Process
GO:0009097	isoleucine biosynthetic process
GO:0009099	L-valine biosynthetic process
GO:0019752	carboxylic acid metabolic process
GO:0034077	butanediol metabolic process

	Cellular Component
GO:0005948	acetolactate synthase complex

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Molecular Function

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Biological Process

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Cellular Component

External links

PDB	RCSB:5wdg, PDBe:5wdg, PDBj:5wdg
PDBsum	5wdg
PubMed
UniProt	P27696\|ILVB_KLEPN Acetolactate synthase, catabolic (Gene Name=budB)

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