Structure of PDB 5wkc Chain B Binding Site BS07

Receptor Information

>5wkc Chain B (length=598) 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
AFEIATSGRPGPVLVDLPKDVTAAILRNPIPTKTTLPTSRAQDEFVMQSI
NKAADLINLAKKPVLYVGAGILNHADGPRLLKELSDRAQIPVTTTLQGLG
SFDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVTGNISKFA
PEARRAAAEGRGGIIHFEVSPKNINKVVQTQIAVEGDATTNLGKMMSKIF
PVKERSEWFAQINKWKKEYPYAYMEETPGSKIKPQTVIKKLSKVANDTGR
HVIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAK
PESLVIDIDGDASFNMTLTELSSAVQAGTPVKILILNNEEQGMVTQWQSL
FYEHRYSHTHQLNPDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGPV
LLEVEVDKKVPVLPMVAGGSGLDEFINFDPEVERQQTELRHKRTGGKH

Ligand information

Ligand ID

TP9

InChI

InChI=1S/C11H20N4O7P2S/c1-7(13-5-9-6-14-8(2)15-11(9)12)10(25)3-4-21-24(19,20)22-23(16,17)18/h6,13,25H,3-5H2,1-2H3,(H,19,20)(H2,12,14,15)(H2,16,17,18)/p-2/b10-7-

InChIKey

WTQDUFKDQLXDPH-YFHOEESVSA-L

SMILES

Software	SMILES
OpenEye OEToolkits 1.5.0	Cc1ncc(c(n1)N)CN/C(=C(/CCO[P@](=O)([O-])O[P@@](=O)(O)[O-])\S)/C
CACTVS 3.341	CC(NCc1cnc(C)nc1N)=C(S)CCO[P]([O-])(=O)O[P](O)([O-])=O
CACTVS 3.341	CC(/NCc1cnc(C)nc1N)=C(/S)CCO[P]([O-])(=O)O[P](O)([O-])=O
OpenEye OEToolkits 1.5.0	Cc1ncc(c(n1)N)CNC(=C(CCOP(=O)([O-])OP(=O)(O)[O-])S)C

Formula

C11 H18 N4 O7 P2 S

Name

(3Z)-4-{[(4-AMINO-2-METHYLPYRIMIDIN-5-YL)METHYL]AMINO}-3-MERCAPTOPENT-3-EN-1-YL TRIHYDROGEN DIPHOSPHATE

ChEMBL

DrugBank

ZINC

PDB chain

5wkc Chain E Residue 704 [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	5wkc Structural insights into the mechanism of inhibition of AHAS by herbicides.
Resolution	2.334 Å
Binding residue (original residue number in PDB)	P114 E139 P165
Binding residue (residue number reindexed from 1)	P32 E57 P83
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)	Y31 G33 G34 A35 I36 E57 T80 F119 Q120 E121 K169 R229 M265 V292 V408 L433 G434 M436 D461 N488 E490 Q491 M493 V494 W497 L519 G524 L525 K558
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:5wkc, PDBe:5wkc, PDBj:5wkc
PDBsum	5wkc
PubMed	29440497
UniProt	P07342\|ILVB_YEAST Acetolactate synthase catalytic subunit, mitochondrial (Gene Name=ILV2)

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