Structure of PDB 6bd9 Chain A

Receptor sequence

>6bd9A (length=542) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]

PDMDTSFVGLTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFN
FVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTPMADAFADGI
PMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINE
AFEIATSGRPGPVLVDLPKDVTAAILRNPIPTKTTLPSNAQDEFVMQSIN
KAADLINLAKKPVLYVGAGILNHADGPRLLKELSDRAQIPVTTTLQGLGS
FDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVTGNISKFAP
EARRAAAEGRGGIIHFEVSPKNINKVVQTQIAVEGDATTNLGKMMSKIFP
VKERSEWFAQINKWKKEYPYAYMEETPGSKIKPQTVIKKLSKVANDTGRH
VIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKP
ESLVIDIDGDASFNMTLTELSSAVQAGTPVKILILNNEESHTHQLNPDFI
KLAEAMGLKGLRVKKQEELDAKLKEFVSTKGPVLLEVEVDKK

3D structure

PDB

6bd9 High resolution crystal structures of the acetohydroxyacid synthase-pyruvate complex provide new insights into its catalytic mechanism

Chain

Resolution

1.982 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 R318 M354 V381 V497 L522 G523 M525 D550 N577 E579 L608 G613 L614 K647
Catalytic site (residue number reindexed from 1)	Y31 G33 G34 A35 I36 E57 T80 F119 Q120 E121 K169 R228 M264 V291 V407 L432 G433 M435 D460 N487 E489 L502 G507 L508 K541
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)
BS01	MG	A	D550 N577	D460 N487
BS02	FAD	A	R241 G307 A308 G309 N312 T334 L335 L352 G353 H355 G374 A375 R376 D378 R380 V381 E407 V408 N412 G425 D426 A427	R159 G217 A218 G219 N222 T244 L245 L262 G263 H265 G284 A285 R286 D288 R290 V291 E317 V318 N322 G335 D336 A337
BS03	TPP	A	V497 G498 Q499 H500 G523 M525 G549 D550 A551 S552 M555 N577	V407 G408 Q409 H410 G433 M435 G459 D460 A461 S462 M465 N487
BS04	PYR	A	G115 G116 Q202	G33 G34 Q120
BS05	PYR	A	G116 A117	G34 A35
BS06	OXY	A	A551 Q600	A461 Q494
BS07	OXY	A	G116 T162 Q202	G34 T80 Q120
BS08	TPP	A	P114 E139	P32 E57

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:6bd9, PDBe:6bd9, PDBj:6bd9
PDBsum	6bd9
PubMed
UniProt	P07342\|ILVB_YEAST Acetolactate synthase catalytic subunit, mitochondrial (Gene Name=ILV2)

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