Structure of PDB 6bd9 Chain B

Receptor sequence

>6bd9B (length=564) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]

PDMDTSFVGLTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFN
FVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTPMADAFADGI
PMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINE
AFEIATSGRPGPVLVDLPKDVTAAILRNPIPTKTTLPSNALNQLTSRAQD
EFVMQSINKAADLINLAKKPVLYVGAGILNHADGPRLLKELSDRAQIPVT
TTLQGLGSFDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVT
GNISKFAPEARRAAAEGRGGIIHFEVSPKNINKVVQTQIAVEGDATTNLG
KMMSKIFPVKERSEWFAQINKWKKEYPYAYMEETPGSKIKPQTVIKKLSK
VANDTGRHVIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAA
IGAQVAKPESLVIDIDGDASFNMTLTELSSAVQAGTPVKILILNNEEQGM
VTQWQSLFYEHRYSHTHQLNPDFIKLAEAMGLKGLRVKKQEELDAKLKEF
VSTKGPVLLEVEVD

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 Q580 M582 V583 W586 L608 G613 L614
Catalytic site (residue number reindexed from 1)	Y31 G33 G34 A35 I36 E57 T80 F119 Q120 E121 K169 R236 M272 V299 V415 L440 G441 M443 D468 N495 E497 Q498 M500 V501 W504 L526 G531 L532
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	TPP	B	P114 E139	P32 E57
BS02	FAD	B	R241 G307 A308 G309 T334 L335 H355 G374 A375 R376 R380 V381 E407 V408 D426 A427 M502 G520	R159 G225 A226 G227 T252 L253 H273 G292 A293 R294 R298 V299 E325 V326 D344 A345 M420 G438
BS03	MG	B	D550 N577	D468 N495
BS04	TPP	B	V497 G498 Q499 H500 G523 M525 G549 D550 A551 S552 M555 N577	V415 G416 Q417 H418 G441 M443 G467 D468 A469 S470 M473 N495
BS05	PYR	B	G116 Q202	G34 Q120
BS06	OXY	B	E578 H599 Q600	E496 H517 Q518
BS07	OXY	B	E578 L601 N602	E496 L519 N520
BS08	OXY	B	G116 A117 T162 Q202	G34 A35 T80 Q120

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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