Structure of PDB 1yhz Chain A

Receptor sequence

>1yhzA (length=582) Species: 3702 (Arabidopsis thaliana) [Search protein sequence]

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

3D structure

PDB

1yhz Herbicide-binding sites revealed in the structure of plant acetohydroxyacid synthase

Chain

Resolution

2.7 Å

3D
structure

Catalytic site residues are labeled in the structure
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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.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)
BS01	MG	A	D538 N565 H567	D453 N480 H482
BS02	1CS	A	D376 R377 M570 W574 S653	D291 R292 M485 W489 S568
BS03	FAD	A	R246 G308 G309 T331 L332 M333 L349 M351 H352 G371 V372 R373 D375 V378 D395 I396 D414 V415 Q489 M490 G508 G509	R161 G223 G224 T246 L247 M248 L264 M266 H267 G286 V287 R288 D290 V293 D310 I311 D329 V330 Q404 M405 G423 G424

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

View graph for
Molecular Function

View graph for
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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