Structure of PDB 6u9d Chain B

Receptor sequence

>6u9dB (length=607) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]

AEPDMDTSFVGLTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDK
FNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTPMADAFAD
GIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRI
NEAFEIATSGRPGPVLVDLPKDVTAAILRNPIPTKTTLPSNALNQLTSRA
QDEFVMQSINKAADLINLAKKPVLYVGAGILNHADGPRLLKELSDRAQIP
VTTTLQGLGSFDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDR
VTGNISKFAPEARRAAAEGRGGIIHFEVSPKNINKVVQTQIAVEGDATTN
LGKMMSKIFPVKERSEWFAQINKWKKEYPYAYMEETPGSKIKPQTVIKKL
SKVANDTGRHVIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLP
AAIGAQVAKPESLVIDIDGDASFNMTLTELSSAVQAGTPVKILILNNEEQ
GMVTQWQSLFYEHRYSHTHQLNPDFIKLAEAMGLKGLRVKKQEELDAKLK
EFVSTKGPVLLEVEVDKKVPVLPMVAGGSGLDEFINFDPEVERQQTELRH
KRTGGKH

3D structure

PDB

6u9d Structures of fungal and plant acetohydroxyacid synthases.

Chain

Resolution

3.194 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 M354 V381 V497 G523 M525 D550 N577 E579 Q580 M582 V583 W586
Catalytic site (residue number reindexed from 1)	Y33 G35 G36 A37 I38 E59 T82 F121 Q122 E123 K171 M274 V301 V417 G443 M445 D470 N497 E499 Q500 M502 V503 W506
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	B	E139 P165	E59 P85
BS02	60G	B	G116 V191 P192 F201 K251	G36 V111 P112 F121 K171	BindingDB: Ki=4.4nM
BS03	TPP	B	V497 G498 Q499 H500 G523 M525 A551 S552 N577 E579 Q580 G581 M582 V583	V417 G418 Q419 H420 G443 M445 A471 S472 N497 E499 Q500 G501 M502 V503
BS04	MG	B	D550 N577	D470 N497
BS05	FAD	B	R241 A308 G309 N312 T334 L335 Q336 L352 M354 G374 R376 D378 R380 V381 E407 V408 N412 D426 A427 M502 G520 G521	R161 A228 G229 N232 T254 L255 Q256 L272 M274 G294 R296 D298 R300 V301 E327 V328 N332 D346 A347 M422 G440 G441
BS06	60G	B	D379 R380 M582 W586	D299 R300 M502 W506	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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component

External links

PDB	RCSB:6u9d, PDBe:6u9d, PDBj:6u9d
PDBsum	6u9d
PubMed	32640464
UniProt	P07342\|ILVB_YEAST Acetolactate synthase catalytic subunit, mitochondrial (Gene Name=ILV2)

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