Structure of PDB 6bd3 Chain B

Receptor sequence

>6bd3B (length=558) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]

DMDTSFVGLTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFNF
VLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTPMADAFADGIP
MVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEA
FEIATSGRPGPVLVDLPKDVTAAILRNPIPTKTTLPSQLTSRAQDEFVMQ
SINKAADLINLAKKPVLYVGAGILNHADGPRLLKELSDRAQIPVTTTLQG
LGSFDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVTGNISK
FAPEARRAAAEGRGGIIHFEVSPKNINKVVQTQIAVEGDATTNLGKMMSK
IFPVKERSEWFAQINKWKKEYPYAYMEETPGSKIKPQTVIKKLSKVANDT
GRHVIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQV
AKPESLVIDIDGDASFNMTLTELSSAVQAGTPVKILILNNEEQGMVTQWQ
SLFYSHTHQLNPDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGPVLL
EVEVDKKV

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 E579 Q580 M582 V583 W586 L608 G613 L614 K647
Catalytic site (residue number reindexed from 1)	Y30 G32 G33 A34 I35 E56 T79 F118 Q119 E120 K168 R231 M267 V294 V410 L435 G436 M438 D463 N490 E492 Q493 M495 V496 W499 L517 G522 L523 K556
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 P165 Q202	P31 E56 P82 Q119
BS02	MG	B	D550 N577	D463 N490
BS03	HTL	B	Q499 H500 G523 M525 G549 D550 A551 S552 M555 N577	Q412 H413 G436 M438 G462 D463 A464 S465 M468 N490
BS04	OXY	B	E578 H599 Q600	E491 H508 Q509
BS05	OXY	B	E578 L601 N602	E491 L510 N511
BS06	OXY	B	G116 A117 T162 S163 Q202	G33 A34 T79 S80 Q119
BS07	FAD	B	R241 G307 A308 G309 N312 T334 L335 L352 H355 G374 A375 R376 D378 R380 V381 E407 V408 D426 A427 Q501 M502 G520	R158 G220 A221 G222 N225 T247 L248 L265 H268 G287 A288 R289 D291 R293 V294 E320 V321 D339 A340 Q414 M415 G433

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

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