Structure of PDB 5wkc Chain B

Receptor sequence

>5wkcB (length=598) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]

PDMDTSFVGLTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFN
FVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTPMADAFADGI
PMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINE
AFEIATSGRPGPVLVDLPKDVTAAILRNPIPTKTTLPTSRAQDEFVMQSI
NKAADLINLAKKPVLYVGAGILNHADGPRLLKELSDRAQIPVTTTLQGLG
SFDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVTGNISKFA
PEARRAAAEGRGGIIHFEVSPKNINKVVQTQIAVEGDATTNLGKMMSKIF
PVKERSEWFAQINKWKKEYPYAYMEETPGSKIKPQTVIKKLSKVANDTGR
HVIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAK
PESLVIDIDGDASFNMTLTELSSAVQAGTPVKILILNNEEQGMVTQWQSL
FYEHRYSHTHQLNPDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGPV
LLEVEVDKKVPVLPMVAGGSGLDEFINFDPEVERQQTELRHKRTGGKH

3D structure

PDB

5wkc Structural insights into the mechanism of inhibition of AHAS by herbicides.

Chain

Resolution

2.334 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 R229 M265 V292 V408 L433 G434 M436 D461 N488 E490 Q491 M493 V494 W497 L519 G524 L525 K558
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	MG	B	D550 N577 E579	D461 N488 E490
BS02	PXD	B	M354 D379 R380 V583 W586	M265 D290 R291 V494 W497	MOAD: Ki=2.2nM
BS03	FAD	B	R241 G307 A308 G309 N312 T334 L335 Q336 L352 G374 A375 R376 R380 V381 E407 V408 D426 A427 M502 G520	R159 G218 A219 G220 N223 T245 L246 Q247 L263 G285 A286 R287 R291 V292 E318 V319 D337 A338 M413 G431
BS04	TP9	B	V497 G498 Q499 H500 M525 G549 D550 A551 S552 M555 N577 E579 Q580 G581 M582 V583	V408 G409 Q410 H411 M436 G460 D461 A462 S463 M466 N488 E490 Q491 G492 M493 V494
BS05	F50	B	G115 G116 Q202	G33 G34 Q120
BS06	PXD	B	G116 A117 V191 F201 K251	G34 A35 V109 F119 K169	MOAD: Ki=2.2nM
BS07	TP9	B	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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component

External links

PDB	RCSB:5wkc, PDBe:5wkc, PDBj:5wkc
PDBsum	5wkc
PubMed	29440497
UniProt	P07342\|ILVB_YEAST Acetolactate synthase catalytic subunit, mitochondrial (Gene Name=ILV2)

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