Structure of PDB 6bd3 Chain A

Receptor sequence

>6bd3A (length=538) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]

PDMDTSFVGLTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFN
FVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTPMADAFADGI
PMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINE
AFEIATSGRPGPVLVDLPKDVTAAILRNPIPTKTTLPSDEFVMQSINKAA
DLINLAKKPVLYVGAGILNHADGPRLLKELSDRAQIPVTTTLQGLGSFDQ
EDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVTGNISKFAPEAR
RAAAEGRGGIIHFEVSPKNINKVVQTQIAVEGDATTNLGKMMSKIFPVKE
RSEWFAQINKWKKEYPYAYMEETPGSKIKPQTVIKKLSKVANDTGRHVIV
TTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESL
VIDIDGDASFNMTLTELSSAVQAGTPVKILILNNESHTHQLNPDFIKLAE
AMGLKGLRVKKQEELDAKLKEFVSTKGPVLLEVEVDKK

3D structure

PDB

6bd3 High resolution crystal structures of the acetohydroxyacid synthase-pyruvate complex provide new insights into its catalytic mechanism

Chain

Resolution

2.28 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 L608 G613 L614 K647
Catalytic site (residue number reindexed from 1)	Y31 G33 G34 A35 I36 E57 T80 F119 Q120 E121 K169 R225 M261 V288 V404 L429 G430 M432 D457 N484 L498 G503 L504 K537
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	D457 N484
BS02	TPP	A	V497 G498 Q499 H500 G523 M525 D550 A551 S552 M555 N577	V404 G405 Q406 H407 G430 M432 D457 A458 S459 M462 N484
BS03	OXY	A	A117 T162 S163 Q202	A35 T80 S81 Q120
BS04	FAD	A	R241 G307 A308 G309 N312 T334 L335 Q336 L352 G353 H355 G374 A375 R376 D378 R380 V381 E407 V408 D426 A427	R159 G214 A215 G216 N219 T241 L242 Q243 L259 G260 H262 G281 A282 R283 D285 R287 V288 E314 V315 D333 A334
BS05	HTL	A	P114 E139 P165	P32 E57 P83

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:6bd3, PDBe:6bd3, PDBj:6bd3
PDBsum	6bd3
PubMed
UniProt	P07342\|ILVB_YEAST Acetolactate synthase catalytic subunit, mitochondrial (Gene Name=ILV2)

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