Structure of PDB 5d6r Chain M Binding Site BS01

Receptor Information
>5d6r Chain M (length=553) 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
AEILRDRQHQRELQLNQFALHPLRIVRAMQDIVNSDVTLTVDMGSFHIWI
ARYLYSFRARQVMISNGQQTMGVALPWAIGAWLVNPERKVVSVSGDGGFL
QSSMELETAVRLKANVLHLIWVDNGYNMVAIQEEKKYQRLSGVEFGPMDF
KAYAESFGAKGFAVESAEALEPTLRAAMDVDGPAVVAIPVDYRDNPLLMG
QLH
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain5d6r Chain M Residue 601 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5d6r Acetolactate Synthase from Klebsiella pneumoniae in Complex with Mechanism-Based Inhibitor
Resolution2.276 Å
Binding residue
(original residue number in PDB)		D447 D474 G476
Binding residue
(residue number reindexed from 1)		D446 D473 G475
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) G34 I37 E57 H119 Q120 S121 Q169 E289 Q420 D447 D474 G476 Y477 M479 V480 Q483 Y543
Catalytic site (residue number reindexed from 1) G39 I42 E62 H124 Q125 S126 Q174 E294 Q419 D446 D473 G475 Y476 M478 V479 Q482 Y542
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:5d6r, PDBe:5d6r, PDBj:5d6r
PDBsum5d6r
PubMed
UniProtP27696|ILVB_KLEPN Acetolactate synthase, catabolic (Gene Name=budB)

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