Structure of PDB 1t9c Chain B

Receptor sequence

>1t9cB (length=593) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]

DMDTSFVGLTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFNF
VLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTPMADAFADGIP
MVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEA
FEIATSGRPGPVLVDLPKDVTAAILRNPIPTKTTLPQDEFVMQSINKAAD
LINLAKKPVLYVGAGILNHADGPRLLKELSDRAQIPVTTTLQGLGSFDQE
DPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVTGNISKFAPEARR
AAAEGRGGIIHFEVSPKNINKVVQTQIAVEGDATTNLGKMMSKIFPVKER
SEWFAQINKWKKEYPYAYMEETPGSKIKPQTVIKKLSKVANDTGRHVIVT
TGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLV
IDIDGDASFNMTLTELSSAVQAGTPVKILILNNEEQGMVTQWQSLFYEHR
YSHTHQLNPDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGPVLLEVE
VDKKVPVLPMVAGGSGLDEFINFDPEVERQQTELRHKRTGGKH

3D structure

PDB

1t9c Elucidating the specificity of binding of sulfonylurea herbicides to acetohydroxyacid synthase.

Chain

Resolution

2.34 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 R224 M260 V287 V403 L428 G429 M431 D456 N483 E485 Q486 M488 V489 W492 L514 G519 L520 K553
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	1SM	B	G116 V191 P192 F201 K251	G33 V108 P109 F118 K168	BindingDB: Ki=51nM
BS02	MG	B	D550 N577 E579	D456 N483 E485
BS03	P23	B	V497 G498 Q499 H500 M525 G549 D550 A551 S552 N577 E579 Q580 G581 M582	V403 G404 Q405 H406 M431 G455 D456 A457 S458 N483 E485 Q486 G487 M488
BS04	1SM	B	D379 R380 M582 W586	D285 R286 M488 W492	BindingDB: Ki=51nM
BS05	FAD	B	R241 G307 A308 G309 N312 T334 L335 L352 M354 H355 G374 A375 R376 D378 R380 V381 E407 V408 N412 D426 A427 Q501 M502 G520 G521 M582	R158 G213 A214 G215 N218 T240 L241 L258 M260 H261 G280 A281 R282 D284 R286 V287 E313 V314 N318 D332 A333 Q407 M408 G426 G427 M488

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

View graph for
Biological Process

View graph for
Cellular Component

External links

PDB	RCSB:1t9c, PDBe:1t9c, PDBj:1t9c
PDBsum	1t9c
PubMed	15709745
UniProt	P07342\|ILVB_YEAST Acetolactate synthase catalytic subunit, mitochondrial (Gene Name=ILV2)

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