Structure of PDB 5fem Chain B Binding Site BS01

Receptor Information

>5fem Chain B (length=599) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

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

Ligand information

Ligand ID

60G

InChI

InChI=1S/C16H18N4O7S/c1-25-12-8-13(26-2)18-15(17-12)19-16(22)20-28(23,24)9-10-6-4-5-7-11(10)14(21)27-3/h4-8H,9H2,1-3H3,(H2,17,18,19,20,22)

InChIKey

XMQFTWRPUQYINF-UHFFFAOYSA-N

SMILES

Software	SMILES
OpenEye OEToolkits 2.0.4	COc1cc(nc(n1)NC(=O)NS(=O)(=O)Cc2ccccc2C(=O)OC)OC
CACTVS 3.385	COC(=O)c1ccccc1C[S](=O)(=O)NC(=O)Nc2nc(OC)cc(OC)n2

Formula

C16 H18 N4 O7 S

Name

methyl 2-[(4,6-dimethoxypyrimidin-2-yl)carbamoylsulfamoylmethyl]benzoate;
Bensulfuron methyl

PDB chain

5fem Chain A Residue 703 [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	5fem Commercial Herbicides Can Trigger the Oxidative Inactivation of Acetohydroxyacid Synthase.
Resolution	2.168 Å
Binding residue (original residue number in PDB)	G116 P192 F201 K251
Binding residue (residue number reindexed from 1)	G34 P110 F119 K169
Annotation score	1
Binding affinity	BindingDB: Ki=4.4nM

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.

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:5fem, PDBe:5fem, PDBj:5fem
PDBsum	5fem
PubMed	26924714
UniProt	P07342\|ILVB_YEAST Acetolactate synthase catalytic subunit, mitochondrial (Gene Name=ILV2)

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