Structure of PDB 6u9d Chain R

Receptor sequence
>6u9dR (length=416) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
DMDTSFVGLTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFNF
VLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTPMADAFADGIP
MVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEA
FEIATSGRPGPVLVDLPKDVTAAILRNPIPTKTTLPSNALNAQDEFVMQS
INKAADLINLAKKPVLYVGAGILNHADGPRLLKELSDRAQTTTLQGLGQN
ADLIIAVGARFDDRVTGNISKFAPEARRAAGIIHFEVSPKNINKVVQTQI
AVEGDATTNLGKMMSKIFPVKEQTVIKKLSKVANDTLGTMGYGLLVIDID
GDASFNMTLTELSSAVQAGTPVKILILNVTQWQSLFYEHRKQEELDAKLK
EFVPVLLEVEVDKKVP
3D structure
PDB6u9d Structures of fungal and plant acetohydroxyacid synthases.
ChainR
Resolution3.194 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 TPP R E139 P165 E56 P82
BS02 60G R G116 V191 P192 F201 K251 G33 V108 P109 F118 K168 BindingDB: Ki=4.4nM
BS03 FAD R R241 G309 N312 T334 L335 Q336 G374 R376 D378 R380 V381 E407 V408 N412 R158 G221 N224 T243 L244 Q245 G258 R260 D262 R264 V265 E286 V287 N291
BS04 60G R R380 W586 R264 W382 BindingDB: Ki=4.4nM
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:6u9d, PDBe:6u9d, PDBj:6u9d
PDBsum6u9d
PubMed32640464
UniProtP07342|ILVB_YEAST Acetolactate synthase catalytic subunit, mitochondrial (Gene Name=ILV2)

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