Structure of PDB 6den Chain A

Receptor sequence

>6denA (length=599) Species: 237561 (Candida albicans SC5314) [Search protein sequence]

KKKEQLMDDSFIGLTGGEIFHEMMLRHKVDTVFGYAGGAILPVFDAIYNS
DKFKFVLPRHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVITPMADAL
MDGVPLVVFSGQVPTTAIGTDAFQEADIVGISRSCTKWNVMVKNVAELPR
RINEAFEIATTGRPGPVLVDLPKDVTASILRESIPINTTLPAVSEFTSEA
IKRAANILNKAKKPIIYAGAGILNNEQGPKLLKELADKANIPVTTTLQGL
GAFDQRDPKSLDMLGMHGSAAANTAIQNADCIIALGARFDDRVTGNISKF
APEAKLAASEGRGGILHFEISPKNINKVVEATEAIEGDVTANLQSFIPLV
DSIENRPEWFNKINEWKKKYPYSYQLETPGSLIKPQTLIKEISDQAQTYN
KEVIVTTGVGQHQMWAAQHFTWTQPRTMITSGGLGTMGYGLPAAIGAQVA
KPDAIVIDIDGDASFNMTLTELSSAVQAGAPIKVCVLNNEEQGMVTQWQS
LFYEHRYSHTHQSNPDFMKLAESMNVKGIRITNQQELKSGVKEFLDATEP
VLLEVIVEKKVPVLPMVPAGKALDDFILWDAEVEKQQNDLRKERTGGKY

3D structure

PDB

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

Chain

Resolution

1.806 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 K230 M266 V293 V409 L434 G435 M437 D462 N489 E491 Q492 M494 V495 W498 L520 N525 V526
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	MG	A	D546 N573 E575	D462 N489 E491
BS02	G8A	A	M350 D375 R376 W582	M266 D291 R292 W498
BS03	FAD	A	R237 G303 A304 G305 N308 T330 L331 Q332 L348 G370 A371 R372 D374 R376 V377 E403 I404 N408 D422 V423 M498 G516	R163 G219 A220 G221 N224 T246 L247 Q248 L264 G286 A287 R288 D290 R292 V293 E319 I320 N324 D338 V339 M414 G432
BS04	TP9	A	V493 G494 Q495 H496 G519 M521 G545 D546 A547 S548 N573 E575 Q576 G577 M578 V579	V409 G410 Q411 H412 G435 M437 G461 D462 A463 S464 N489 E491 Q492 G493 M494 V495

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

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