Structure of PDB 1jsc Chain A Binding Site BS02

Receptor Information
>1jsc Chain A (length=541) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PDMDTSFVGLTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFN
FVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTPMADAFADGI
PMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINE
AFEIATSGRPGPVLVDLPKDVTAAILRNPIPTKTTLPSAQDEFVMQSINK
AADLINLAKKPVLYVGAGILNHADGPRLLKELSDRAQIPVTTTLQGLGSF
DQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVTGNISKFAPE
ARRAAAEGRGGIIHFEVSPKNINKVVQTQIAVEGDATTNLGKMMSKIFPV
KERSEWFAQINKWKKEYPYAYMEETPGSKIKPQTVIKKLSKVANDTGRHV
IVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPE
SLVIDIDGDASFNMTLTELSSAVQAGTPVKILILNNEESHTHQLNPDFIK
LAEAMGLKGLRVKKQEELDAKLKEFVSTKGPVLLEVEVDKK
Ligand information
Ligand ID2HP
InChIInChI=1S/H3O4P/c1-5(2,3)4/h(H3,1,2,3,4)/p-1
InChIKeyNBIIXXVUZAFLBC-UHFFFAOYSA-M
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0OP(=O)(O)[O-]
ACDLabs 10.04[O-]P(=O)(O)O
CACTVS 3.341O[P](O)([O-])=O
FormulaH2 O4 P
NameDIHYDROGENPHOSPHATE ION
ChEMBL
DrugBankDB02831
ZINC
PDB chain1jsc Chain A Residue 698 [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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PDB1jsc Crystal structure of yeast acetohydroxyacid synthase: a target for herbicidal inhibitors.
Resolution2.6 Å
Binding residue
(original residue number in PDB)		G115 G116 Q202
Binding residue
(residue number reindexed from 1)		G33 G34 Q120
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) Y113 G115 G116 A117 I118 E139 T162 F201 Q202 E203 K251 M354 V381 V497 G523 M525 D550 N577 E579 K647
Catalytic site (residue number reindexed from 1) Y31 G33 G34 A35 I36 E57 T80 F119 Q120 E121 K169 M263 V290 V406 G432 M434 D459 N486 E488 K540
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:1jsc, PDBe:1jsc, PDBj:1jsc
PDBsum1jsc
PubMed11902841
UniProtP07342|ILVB_YEAST Acetolactate synthase catalytic subunit, mitochondrial (Gene Name=ILV2)

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