Structure of PDB 1yhz Chain A Binding Site BS01

Receptor Information

>1yhz Chain A (length=582) Species: 3702 (Arabidopsis thaliana) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

TFISRFAPDQPRKGADILVEALERQGVETVFAYPGGASMEIHQALTRSSS
IRNVLPRHEQGGVFAAEGYARSSGKPGICIATSGPGATNLVSGLADALLD
SVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRII
EEAFFLATSGRPGPVLVDVPKDIQQQLAIPNWEQAMRLPGYMSRMPKPPE
DSHLEQIVRLISESKKPVLYVGGGCLNSSDELGRFVELTGIPVASTLMGL
GSYPCDDELSLHMLGMHGTVYANYAVEHSDLLLAFGVRFDDRVTGKLEAF
ASRAKIVHIDIDSAEIGKNKTPHVSVCGDVKLALQGMNKVLENRAEELKL
DFGVWRNELNVQKQKFPLSFKTFGEAIPPQYAIKVLDELTDGKAIISTGV
GQHQMWAAQFYNYKKPRQWLSSGGLGAMGFGLPAAIGASVANPDAIVVDI
DGDGSFIMNVQELATIRVENLPVKVLLLNNQHLGMVMQWEDRFYKANRAH
TFLGDPAQEDEIFPNMLLFAAACGIPAARVTKKADLREAIQTMLDTPGPY
LLDVICPHQEHVLPMIPSGGTFNDVITEGDGR

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

1yhz 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	1yhz Herbicide-binding sites revealed in the structure of plant acetohydroxyacid synthase
Resolution	2.7 Å
Binding residue (original residue number in PDB)	D538 N565 H567
Binding residue (residue number reindexed from 1)	D453 N480 H482
Annotation score	1

Enzymatic activity

Catalytic site (original residue number in PDB)	Y118 G120 G121 A122 S123 E144 T167 F206 Q207 E208 K256 M351 V378 V485 G511 M513 D538 N565 H567 L568 M570 V571 W574 H643
Catalytic site (residue number reindexed from 1)	Y33 G35 G36 A37 S38 E59 T82 F121 Q122 E123 K171 M266 V293 V400 G426 M428 D453 N480 H482 L483 M485 V486 W489 H558
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:0030976	thiamine pyrophosphate binding
GO:0050660	flavin adenine dinucleotide binding

	Biological Process
GO:0009082	branched-chain amino acid biosynthetic process

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Molecular Function

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Biological Process

External links

PDB	RCSB:1yhz, PDBe:1yhz, PDBj:1yhz
PDBsum	1yhz
PubMed	16407096
UniProt	P17597\|ILVB_ARATH Acetolactate synthase, chloroplastic (Gene Name=ALS)

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