Structure of PDB 1t9a Chain A

Receptor sequence

>1t9aA (length=597) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]

DMDTSFVGLTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFNF
VLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTPMADAFADGIP
MVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEA
FEIATSGRPGPVLVDLPKDVTAAILRNPIPTKTTLPTSRAQDEFVMQSIN
KAADLINLAKKPVLYVGAGILNHADGPRLLKELSDRAQIPVTTTLQGLGS
FDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVTGNISKFAP
EARRAAAEGRGGIIHFEVSPKNINKVVQTQIAVEGDATTNLGKMMSKIFP
VKERSEWFAQINKWKKEYPYAYMEETPGSKIKPQTVIKKLSKVANDTGRH
VIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKP
ESLVIDIDGDASFNMTLTELSSAVQAGTPVKILILNNEEQGMVTQWQSLF
YEHRYSHTHQLNPDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGPVL
LEVEVDKKVPVLPMVAGGSGLDEFINFDPEVERQQTELRHKRTGGKH

3D structure

PDB

1t9a Elucidating the specificity of binding of sulfonylurea herbicides to acetohydroxyacid synthase.

Chain

Resolution

2.59 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	Y113 G115 G116 A117 I118 E139 T162 F201 Q202 E203 K251 R318 M354 V381 V497 L522 G523 M525 D550 N577 E579 Q580 M582 V583 W586 L608 G613 L614 K647
Catalytic site (residue number reindexed from 1)	Y30 G32 G33 A34 I35 E56 T79 F118 Q119 E120 K168 R228 M264 V291 V407 L432 G433 M435 D460 N487 E489 Q490 M492 V493 W496 L518 G523 L524 K557
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)	Binding affinity
BS01	MG	A	D550 N577 E579	D460 N487 E489
BS02	1TB	A	M354 D379 R380 M582 V583 W586	M264 D289 R290 M492 V493 W496	BindingDB: Ki=400nM
BS03	FAD	A	R241 G307 A308 G309 N312 T334 L335 Q336 L352 M354 H355 G374 A375 R376 D378 R380 V381 E407 V408 N412 G425 D426 A427 Q501 M502 G520 G521	R158 G217 A218 G219 N222 T244 L245 Q246 L262 M264 H265 G284 A285 R286 D288 R290 V291 E317 V318 N322 G335 D336 A337 Q411 M412 G430 G431
BS04	P23	A	V497 G498 Q499 H500 M525 G549 D550 A551 S552 N577 E579 Q580 G581 M582	V407 G408 Q409 H410 M435 G459 D460 A461 S462 N487 E489 Q490 G491 M492
BS05	1TB	A	G116 V191 P192 F201 K251	G33 V108 P109 F118 K168	BindingDB: Ki=400nM
BS06	YF4	A	G523 M525 M555	G433 M435 M465

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:0008652	amino acid biosynthetic process
GO:0009082	branched-chain amino acid biosynthetic process
GO:0009097	isoleucine biosynthetic process
GO:0009099	L-valine biosynthetic process

	Cellular Component
GO:0005739	mitochondrion
GO:0005948	acetolactate synthase complex

View graph for
Molecular Function

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Biological Process

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Cellular Component

External links

PDB	RCSB:1t9a, PDBe:1t9a, PDBj:1t9a
PDBsum	1t9a
PubMed	15709745
UniProt	P07342\|ILVB_YEAST Acetolactate synthase catalytic subunit, mitochondrial (Gene Name=ILV2)

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