Structure of PDB 1n0h Chain A

Receptor sequence

>1n0hA (length=599) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]

PDMDTSFVGLTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFN
FVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTPMADAFADGI
PMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINE
AFEIATSGRPGPVLVDLPKDVTAAILRNPIPTKTTLPSTSRAQDEFVMQS
INKAADLINLAKKPVLYVGAGILNHADGPRLLKELSDRAQIPVTTTLQGL
GSFDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVTGNISKF
APEARRAAAEGRGGIIHFEVSPKNINKVVQTQIAVEGDATTNLGKMMSKI
FPVKERSEWFAQINKWKKEYPYAYMEETPGSKIKPQTVIKKLSKVANDTG
RHVIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVA
KPESLVIDIDGDASFNMTLTELSSAVQAGTPVKILILNNEEQGMVTQWQS
LFYEHRYSHTHQLNPDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGP
VLLEVEVDKKVPVLPMVAGGSGLDEFINFDPEVERQQTELRHKRTGGKH

3D structure

PDB

1n0h Molecular basis of sulfonylurea herbicide inhibition of acetohydroxyacid synthase

Chain

Resolution

2.8 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)	Y31 G33 G34 A35 I36 E57 T80 F119 Q120 E121 K169 R230 M266 V293 V409 L434 G435 M437 D462 N489 E491 Q492 M494 V495 W498 L520 G525 L526 K559
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	D462 N489 E491
BS02	CIE	A	M354 D379 R380 V583 W586	M266 D291 R292 V495 W498	BindingDB: Ki=3.3nM
BS03	AYD	A	V497 G498 Q499 H500 G523 M525 G549 D550 A551 S552 M555 N577 E579 Q580 G581 V583	V409 G410 Q411 H412 G435 M437 G461 D462 A463 S464 M467 N489 E491 Q492 G493 V495
BS04	FAD	A	R241 G307 A308 G309 N312 T334 L335 Q336 L352 G353 M354 H355 G374 A375 R376 D378 R380 V381 E407 V408 N412 G425 D426 A427 M502 G520 G521	R159 G219 A220 G221 N224 T246 L247 Q248 L264 G265 M266 H267 G286 A287 R288 D290 R292 V293 E319 V320 N324 G337 D338 A339 M414 G432 G433
BS05	CIE	A	G116 A117 V191 P192 F201 K251	G34 A35 V109 P110 F119 K169	BindingDB: Ki=3.3nM
BS06	TPP	A	Y113 E139 P165	Y31 E57 P83

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

View graph for
Cellular Component

External links

PDB	RCSB:1n0h, PDBe:1n0h, PDBj:1n0h
PDBsum	1n0h
PubMed	14557277
UniProt	P07342\|ILVB_YEAST Acetolactate synthase catalytic subunit, mitochondrial (Gene Name=ILV2)

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