Structure of PDB 1t9c Chain A Binding Site BS02

Receptor Information

>1t9c Chain A (length=596) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

MDTSFVGLTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFNFV
LPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTPMADAFADGIPM
VVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAF
EIATSGRPGPVLVDLPKDVTAAILRNPIPTKTTLPSSRAQDEFVMQSINK
AADLINLAKKPVLYVGAGILNHADGPRLLKELSDRAQIPVTTTLQGLGSF
DQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVTGNISKFAPE
ARRAAAEGRGGIIHFEVSPKNINKVVQTQIAVEGDATTNLGKMMSKIFPV
KERSEWFAQINKWKKEYPYAYMEETPGSKIKPQTVIKKLSKVANDTGRHV
IVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPE
SLVIDIDGDASFNMTLTELSSAVQAGTPVKILILNNEEQGMVTQWQSLFY
EHRYSHTHQLNPDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGPVLL
EVEVDKKVPVLPMVAGGSGLDEFINFDPEVERQQTELRHKRTGGKH

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)	D379 R380 W586
Binding residue (residue number reindexed from 1)	D288 R289 W495
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)	Y29 G31 G32 A33 I34 E55 T78 F117 Q118 E119 K167 R227 M263 V290 V406 L431 G432 M434 D459 N486 E488 Q489 M491 V492 W495 L517 G522 L523 K556
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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