Structure of PDB 1t9c Chain B Binding Site BS01

Receptor Information

>1t9c Chain B (length=593) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

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

Ligand information

Ligand ID

1SM

InChI

InChI=1S/C15H16N4O5S/c1-9-8-10(2)17-14(16-9)18-15(21)19-25(22,23)12-7-5-4-6-11(12)13(20)24-3/h4-8H,1-3H3,(H2,16,17,18,19,21)

InChIKey

ZDXMLEQEMNLCQG-UHFFFAOYSA-N

SMILES

Software	SMILES
OpenEye OEToolkits 1.5.0	Cc1cc(nc(n1)NC(=O)NS(=O)(=O)c2ccccc2C(=O)OC)C
CACTVS 3.341	COC(=O)c1ccccc1[S](=O)(=O)NC(=O)Nc2nc(C)cc(C)n2
ACDLabs 10.04	O=C(Nc1nc(cc(n1)C)C)NS(=O)(=O)c2ccccc2C(=O)OC

Formula

C15 H16 N4 O5 S

Name

METHYL 2-[({[(4,6-DIMETHYLPYRIMIDIN-2-YL)AMINO]CARBONYL}AMINO)SULFONYL]BENZOATE;
SULFOMETURON METHYL

PDB chain

1t9c Chain A Residue 695 [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	1t9c Elucidating the specificity of binding of sulfonylurea herbicides to acetohydroxyacid synthase.
Resolution	2.34 Å
Binding residue (original residue number in PDB)	G116 V191 P192 F201 K251
Binding residue (residue number reindexed from 1)	G33 V108 P109 F118 K168
Annotation score	1
Binding affinity	BindingDB: Ki=51nM

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.

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

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Molecular Function

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Biological Process

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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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