Structure of PDB 5fem Chain B

Receptor sequence

>5femB (length=599) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]

PDMDTSFVGLTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFN
FVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTPMADAFADGI
PMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINE
AFEIATSGRPGPVLVDLPKDVTAAILRNPIPTKTTLPSTSRAQDEFVMQS
INKAADLINLAKKPVLYVGAGILNHADGPRLLKELSDRAQIPVTTTLQGL
GSFDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVTGNISKF
APEARRAAAEGRGGIIHFEVSPKNINKVVQTQIAVEGDATTNLGKMMSKI
FPVKERSEWFAQINKWKKEYPYAYMEETPGSKIKPQTVIKKLSKVANDTG
RHVIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVA
KPESLVIDIDGDASFNMTLTELSSAVQAGTPVKILILNNEEQGMVTQWQS
LFYEHRYSHTHQLNPDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGP
VLLEVEVDKKVPVLPMVAGGSGLDEFINFDPEVERQQTELRHKRTGGKH

3D structure

PDB

5fem Commercial Herbicides Can Trigger the Oxidative Inactivation of Acetohydroxyacid Synthase.

Chain

Resolution

2.168 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)	Y31 G33 G34 A35 I36 E57 T80 F119 Q120 E121 K169 R230 M266 V293 V409 L434 G435 M437 D462 N489 E491 Q492 M494 V495 W498 L520 G525 L526 K559
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	60G	B	G116 P192 F201 K251	G34 P110 F119 K169	BindingDB: Ki=4.4nM
BS02	TPP	B	P114 E139 P165	P32 E57 P83
BS03	FAD	B	R241 G307 A308 G309 N312 T334 L335 Q336 L352 G374 A375 R376 R380 V381 E407 V408 N412 G425 D426 A427 M502 G520 G521	R159 G219 A220 G221 N224 T246 L247 Q248 L264 G286 A287 R288 R292 V293 E319 V320 N324 G337 D338 A339 M414 G432 G433
BS04	MG	B	D550 N577 E579	D462 N489 E491
BS05	60G	B	M354 R380 M582 W586	M266 R292 M494 W498	BindingDB: Ki=4.4nM
BS06	MG	B	Q343 D350 Q506 W508	Q255 D262 Q418 W420
BS07	TPP	B	V497 G498 Q499 H500 G523 M525 G549 D550 A551 S552 N577 E579 Q580 G581 M582 V583	V409 G410 Q411 H412 G435 M437 G461 D462 A463 S464 N489 E491 Q492 G493 M494 V495

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

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Biological Process

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Cellular Component

External links

PDB	RCSB:5fem, PDBe:5fem, PDBj:5fem
PDBsum	5fem
PubMed	26924714
UniProt	P07342\|ILVB_YEAST Acetolactate synthase catalytic subunit, mitochondrial (Gene Name=ILV2)

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