Structure of PDB 6deo Chain A

Receptor sequence

>6deoA (length=593) Species: 237561 (Candida albicans SC5314) [Search protein sequence]

QLMDDSFIGLTGGEIFHEMMLRHKVDTVFGYAGGAILPVFDAIYNSDKFK
FVLPRHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVITPMADALMDGV
PLVVFSGQVPTTAIGTDAFQEADIVGISRSCTKWNVMVKNVAELPRRINE
AFEIATTGRPGPVLVDLPKDVTASILRESIPINTTLPSEFTSEAIKRAAN
ILNKAKKPIIYAGAGILNNEQGPKLLKELADKANIPVTTTLQGLGAFDQR
DPKSLDMLGMHGSAAANTAIQNADCIIALGARFDDRVTGNISKFAPEAKL
AASEGRGGILHFEISPKNINKVVEATEAIEGDVTANLQSFIPLVDSIENR
PEWFNKINEWKKKYPYSYQLETPGSLIKPQTLIKEISDQAQTYNKEVIVT
TGVGQHQMWAAQHFTWTQPRTMITSGGLGTMGYGLPAAIGAQVAKPDAIV
IDIDGDASFNMTLTELSSAVQAGAPIKVCVLNNEEQGMVTQWQSLFYEHR
YSHTHQSNPDFMKLAESMNVKGIRITNQQELKSGVKEFLDATEPVLLEVI
VEKKVPVLPMVPAGKALDDFILWDAEVEKQQNDLRKERTGGKY

3D structure

PDB

6deo Commercial AHAS-inhibiting herbicides are promising drug leads for the treatment of human fungal pathogenic infections.

Chain

Resolution

1.971 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	Y109 G111 G112 A113 I114 E135 T158 F197 Q198 E199 K247 K314 M350 V377 V493 L518 G519 M521 D546 N573 E575 Q576 M578 V579 W582 L604 N609 V610
Catalytic site (residue number reindexed from 1)	Y31 G33 G34 A35 I36 E57 T80 F119 Q120 E121 K169 K224 M260 V287 V403 L428 G429 M431 D456 N483 E485 Q486 M488 V489 W492 L514 N519 V520
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	FAD	A	R237 G303 A304 G305 N308 T330 L331 Q332 L348 G370 A371 R372 D374 R376 V377 E403 I404 N408 D422 V423 M498 G516	R159 G213 A214 G215 N218 T240 L241 Q242 L258 G280 A281 R282 D284 R286 V287 E313 I314 N318 D332 V333 M408 G426
BS02	MG	A	D546 N573 E575	D456 N483 E485
BS03	TP9	A	V493 G494 Q495 H496 G519 M521 G545 D546 A547 S548 M551 N573 E575 Q576 G577 M578 V579	V403 G404 Q405 H406 G429 M431 G455 D456 A457 S458 M461 N483 E485 Q486 G487 M488 V489
BS04	H4V	A	M350 D375 R376 M578 W582	M260 D285 R286 M488 W492

Gene Ontology

	Molecular Function
GO:0000166	nucleotide binding
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:0000463	maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
GO:0006412	translation
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
GO:0030150	protein import into mitochondrial matrix

	Cellular Component
GO:0005948	acetolactate synthase complex

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component

External links

PDB	RCSB:6deo, PDBe:6deo, PDBj:6deo
PDBsum	6deo
PubMed	30249642
UniProt	A0A1D8PJF9

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