Structure of PDB 1t9a Chain A Binding Site BS05

Receptor Information

>1t9a Chain A (length=597) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

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

Ligand information

Ligand ID

1TB

InChI

InChI=1S/C15H17N5O6S/c1-9-16-13(18-14(17-9)26-4)20(2)15(22)19-27(23,24)11-8-6-5-7-10(11)12(21)25-3/h5-8H,1-4H3,(H,19,22)

InChIKey

VLCQZHSMCYCDJL-UHFFFAOYSA-N

SMILES

Software	SMILES
OpenEye OEToolkits 1.5.0	Cc1nc(nc(n1)OC)N(C)C(=O)NS(=O)(=O)c2ccccc2C(=O)OC
ACDLabs 10.04	O=C(OC)c1ccccc1S(=O)(=O)NC(=O)N(c2nc(nc(OC)n2)C)C
CACTVS 3.341	COC(=O)c1ccccc1[S](=O)(=O)NC(=O)N(C)c2nc(C)nc(OC)n2

Formula

C15 H17 N5 O6 S

Name

METHYL 2-[4-METHOXY-6-METHYL-1,3,5-TRAZIN-2-YL(METHYL)CARBAMOYLSULFAMOYL]BENZOATE;
TRIBENURON METHYL

PDB chain

1t9a Chain B Residue 1695 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

Global view

Local view

Structure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]

PDB	1t9a Elucidating the specificity of binding of sulfonylurea herbicides to acetohydroxyacid synthase.
Resolution	2.59 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=400nM

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.

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

[Back to BioLiP]