Structure of PDB 6u9d Chain R Binding Site BS01

Receptor Information
>6u9d Chain R (length=416) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DMDTSFVGLTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFNF
VLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTPMADAFADGIP
MVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEA
FEIATSGRPGPVLVDLPKDVTAAILRNPIPTKTTLPSNALNAQDEFVMQS
INKAADLINLAKKPVLYVGAGILNHADGPRLLKELSDRAQTTTLQGLGQN
ADLIIAVGARFDDRVTGNISKFAPEARRAAGIIHFEVSPKNINKVVQTQI
AVEGDATTNLGKMMSKIFPVKEQTVIKKLSKVANDTLGTMGYGLLVIDID
GDASFNMTLTELSSAVQAGTPVKILILNVTQWQSLFYEHRKQEELDAKLK
EFVPVLLEVEVDKKVP
Ligand information
Ligand IDTPP
InChIInChI=1S/C12H18N4O7P2S/c1-8-11(3-4-22-25(20,21)23-24(17,18)19)26-7-16(8)6-10-5-14-9(2)15-12(10)13/h5,7H,3-4,6H2,1-2H3,(H4-,13,14,15,17,18,19,20,21)/p+1
InChIKeyAYEKOFBPNLCAJY-UHFFFAOYSA-O
SMILES
SoftwareSMILES
CACTVS 3.341Cc1ncc(C[n+]2csc(CCO[P@@](O)(=O)O[P](O)(O)=O)c2C)c(N)n1
OpenEye OEToolkits 1.5.0Cc1c(sc[n+]1Cc2cnc(nc2N)C)CCO[P@](=O)(O)OP(=O)(O)O
OpenEye OEToolkits 1.5.0Cc1c(sc[n+]1Cc2cnc(nc2N)C)CCOP(=O)(O)OP(=O)(O)O
CACTVS 3.341Cc1ncc(C[n+]2csc(CCO[P](O)(=O)O[P](O)(O)=O)c2C)c(N)n1
ACDLabs 10.04O=P(O)(O)OP(=O)(O)OCCc1sc[n+](c1C)Cc2c(nc(nc2)C)N
FormulaC12 H19 N4 O7 P2 S
NameTHIAMINE DIPHOSPHATE
ChEMBLCHEMBL1236376
DrugBank
ZINCZINC000008215517
PDB chain6u9d Chain Q Residue 701 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB6u9d Structures of fungal and plant acetohydroxyacid synthases.
Resolution3.194 Å
Binding residue
(original residue number in PDB)		E139 P165
Binding residue
(residue number reindexed from 1)		E56 P82
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) Y113 G115 G116 A117 I118 E139 T162 F201 Q202 E203 K251 V381 G523 M525 D550 V583 W586
Catalytic site (residue number reindexed from 1) Y30 G32 G33 A34 I35 E56 T79 F118 Q119 E120 K168 V265 G338 M340 D352 V379 W382
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
View graph for
Cellular Component
External links
PDB RCSB:6u9d, PDBe:6u9d, PDBj:6u9d
PDBsum6u9d
PubMed32640464
UniProtP07342|ILVB_YEAST Acetolactate synthase catalytic subunit, mitochondrial (Gene Name=ILV2)

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