Structure of PDB 1t9b Chain B Binding Site BS02

Receptor Information

>1t9b Chain B (length=595) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

MDTSFVGLTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFNFV
LPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTPMADAFADGIPM
VVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAF
EIATSGRPGPVLVDLPKDVTAAILRNPIPTKTTLPSRAQDEFVMQSINKA
ADLINLAKKPVLYVGAGILNHADGPRLLKELSDRAQIPVTTTLQGLGSFD
QEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVTGNISKFAPEA
RRAAAEGRGGIIHFEVSPKNINKVVQTQIAVEGDATTNLGKMMSKIFPVK
ERSEWFAQINKWKKEYPYAYMEETPGSKIKPQTVIKKLSKVANDTGRHVI
VTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPES
LVIDIDGDASFNMTLTELSSAVQAGTPVKILILNNEEQGMVTQWQSLFYE
HRYSHTHQLNPDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGPVLLE
VEVDKKVPVLPMVAGGSGLDEFINFDPEVERQQTELRHKRTGGKH

Ligand information

Ligand ID

InChI

InChI=1S/Mg/q+2

InChIKey

JLVVSXFLKOJNIY-UHFFFAOYSA-N

SMILES

Software	SMILES
ACDLabs 10.04 OpenEye OEToolkits 1.5.0	[Mg+2]
CACTVS 3.341	[Mg++]

Formula

Name

MAGNESIUM ION

PDB chain

1t9b Chain B Residue 699 [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	1t9b Elucidating the specificity of binding of sulfonylurea herbicides to acetohydroxyacid synthase.
Resolution	2.2 Å
Binding residue (original residue number in PDB)	D550 N577 E579
Binding residue (residue number reindexed from 1)	D458 N485 E487
Annotation score	1

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 R226 M262 V289 V405 L430 G431 M433 D458 N485 E487 Q488 M490 V491 W494 L516 G521 L522 K555
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:1t9b, PDBe:1t9b, PDBj:1t9b
PDBsum	1t9b
PubMed	15709745
UniProt	P07342\|ILVB_YEAST Acetolactate synthase catalytic subunit, mitochondrial (Gene Name=ILV2)

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