Structure of PDB 6der Chain A

Receptor sequence

>6derA (length=600) Species: 237561 (Candida albicans SC5314) [Search protein sequence]

KKKEQLMDDSFIGLTGGEIFHEMMLRHKVDTVFGYAGGAILPVFDAIYNS
DKFKFVLPRHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVITPMADAL
MDGVPLVVFSGQVPTTAIGTDAFQEADIVGISRSCTKWNVMVKNVAELPR
RINEAFEIATTGRPGPVLVDLPKDVTASILRESIPINTTLPSAVSEFTSE
AIKRAANILNKAKKPIIYAGAGILNNEQGPKLLKELADKANIPVTTTLQG
LGAFDQRDPKSLDMLGMHGSAAANTAIQNADCIIALGARFDDRVTGNISK
FAPEAKLAASEGRGGILHFEISPKNINKVVEATEAIEGDVTANLQSFIPL
VDSIENRPEWFNKINEWKKKYPYSYQLETPGSLIKPQTLIKEISDQAQTY
NKEVIVTTGVGQHQMWAAQHFTWTQPRTMITSGGLGTMGYGLPAAIGAQV
AKPDAIVIDIDGDASFNMTLTELSSAVQAGAPIKVCVLNNEEQGMVTQWQ
SLFYEHRYSHTHQSNPDFMKLAESMNVKGIRITNQQELKSGVKEFLDATE
PVLLEVIVEKKVPVLPMVPAGKALDDFILWDAEVEKQQNDLRKERTGGKY

3D structure

PDB

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

Chain

Resolution

2.126 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 K231 M267 V294 V410 L435 G436 M438 D463 N490 E492 Q493 M495 V496 W499 L521 N526 V527
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 H351 G370 A371 R372 D374 R376 V377 E403 I404 N408 G421 D422 V423 Q497 M498 G516	R163 G220 A221 G222 N225 T247 L248 Q249 L265 H268 G287 A288 R289 D291 R293 V294 E320 I321 N325 G338 D339 V340 Q414 M415 G433
BS02	MG	A	D546 N573 E575	D463 N490 E492
BS03	G87	A	R376 M578 W582 A653	R293 M495 W499 A570
BS04	TZD	A	V493 G494 Q495 H496 G519 M521 G545 D546 A547 S548 M551 N573 E575 Q576 G577 V579	V410 G411 Q412 H413 G436 M438 G462 D463 A464 S465 M468 N490 E492 Q493 G494 V496
BS05	TP9	A	V493 G494 Q495 H496 G519 M521 G545 D546 A547 S548 N573 E575 Q576 G577 M578 V579	V410 G411 Q412 H413 G436 M438 G462 D463 A464 S465 N490 E492 Q493 G494 M495 V496

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

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Molecular Function

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Biological Process

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Cellular Component

External links

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

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