Structure of PDB 1ozg Chain A Binding Site BS02

Receptor Information

>1ozg Chain A (length=549) Species: 573 (Klebsiella pneumoniae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

PVRQWAHGADLVVSQLEAQGVRQVFGIPGAKIDKVFDSLLDSSIRIIPVR
HEANAAFMAAAVGRITGKAGVALVTSGPGCSNLITGMATANSEGDPVVAL
GGAVKRADKAKQVHQSMDTVAMFSPVTKYAIEVTAPDALAEVVSNAFRAA
EQGRPGSAFVSLPQDVVDGPVSGKVLPASGAPQMGAAPDDAIDQVAKLIA
QAKNPIFLLGLMASQPENSKALRRLLETSHIPVTSTYQAAGAVNQDNFSR
FAGRVGLFNNQAGDRLLQLADLVICIGYSPVEYEPAMWNSGNATLVHIDV
LPAYEERNYTPDVELVGDIAGTLNKLAQNIDHRLVLSPQAAEILRDRQHQ
RELLDRRGAQLNQFALHPLRIVRAMQDIVNSDVTLTVDMGSFHIWIARYL
YTFRARQVMISNGQQTMGVALPWAIGAWLVNPERKVVSVSGDGGFLQSSM
ELETAVRLKANVLHLIWVDNGYNMVAIQEEKKYQRLSGVEFGPMDFKAYA
ESFGAKGFAVESAEALEPTLRAAMDVDGPAVVAIPVDYRDNPLLMGQLH

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

1ozg Chain A Residue 699 [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	1ozg The Crystal Structures of Klebsiella pneumoniae Acetolactate Synthase with Enzyme-bound Cofactor and with an Unusual Intermediate.
Resolution	2.3 Å
Binding residue (original residue number in PDB)	D447 D474 G476
Binding residue (residue number reindexed from 1)	D442 D469 G471
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)	I27 G29 A30 K31 I32 E52 T75 H114 Q115 S116 Q164 L257 E284 M389 Q415 M417 D442 D469 G471 Y472 M474 V475 Q478 Y538
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:1ozg, PDBe:1ozg, PDBj:1ozg
PDBsum	1ozg
PubMed	14557277
UniProt	P27696\|ILVB_KLEPN Acetolactate synthase, catabolic (Gene Name=budB)

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