Structure of PDB 6deq Chain A

Receptor sequence

>6deqA (length=601) Species: 237561 (Candida albicans SC5314) [Search protein sequence]

KKKEQLMDDSFIGLTGGEIFHEMMLRHKVDTVFGYAGGAILPVFDAIYNS
DKFKFVLPRHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVITPMADAL
MDGVPLVVFSGQVPTTAIGTDAFQEADIVGISRSCTKWNVMVKNVAELPR
RINEAFEIATTGRPGPVLVDLPKDVTASILRESIPINTTLPSNAVSEFTS
EAIKRAANILNKAKKPIIYAGAGILNNEQGPKLLKELADKANIPVTTTLQ
GLGAFDQRDPKSLDMLGMHGSAAANTAIQNADCIIALGARFDDRVTGNIS
KFAPEAKLAASEGRGGILHFEISPKNINKVVEATEAIEGDVTANLQSFIP
LVDSIENRPEWFNKINEWKKKYPYSYQLETPGSLIKPQTLIKEISDQAQT
YNKEVIVTTGVGQHQMWAAQHFTWTQPRTMITSGGLGTMGYGLPAAIGAQ
VAKPDAIVIDIDGDASFNMTLTELSSAVQAGAPIKVCVLNNEEQGMVTQW
QSLFYEHRYSHTHQSNPDFMKLAESMNVKGIRITNQQELKSGVKEFLDAT
EPVLLEVIVEKKVPVLPMVPAGKALDDFILWDAEVEKQQNDLRKERTGGK
Y

3D structure

PDB

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

Chain

Resolution

2.127 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)	Y35 G37 G38 A39 I40 E61 T84 F123 Q124 E125 K173 K232 M268 V295 V411 L436 G437 M439 D464 N491 E493 Q494 M496 V497 W500 L522 N527 V528
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 D422 V423 M498 G516	R163 G221 A222 G223 N226 T248 L249 Q250 L266 G288 A289 R290 D292 R294 V295 E321 I322 D340 V341 M416 G434
BS02	MG	A	D546 N573 E575	D464 N491 E493
BS03	PXD	A	M350 R376 M578 V579 W582 A653	M268 R294 M496 V497 W500 A571
BS04	TP9	A	V493 G494 Q495 H496 M521 G545 D546 A547 S548 N573 E575 Q576 G577 M578 V579	V411 G412 Q413 H414 M439 G463 D464 A465 S466 N491 E493 Q494 G495 M496 V497

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:6deq, PDBe:6deq, PDBj:6deq
PDBsum	6deq
PubMed	30249642
UniProt	A0A1D8PJF9

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