Structure of PDB 6dek Chain A

Receptor sequence

>6dekA (length=595) Species: 237561 (Candida albicans SC5314) [Search protein sequence]

KKEQLMDDSFIGLTGGEIFHEMMLRHKVDTVFGYAGGAILPVFDAIYNSD
KFKFVLPRHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVITPMADALM
DGVPLVVFSGQVPTTAIQEADIVGISRSCTKWNVMVKNVAELPRRINEAF
EIATTGRPGPVLVDLPKDVTASILRESIPINTTLPSNAVSEFTSEAIKRA
ANILNKAKKPIIYAGAGILNNEQGPKLLKELADKANIPVTTTLQGLGAFD
QRDPKSLDMLGMHGSAAANTAIQNADCIIALGARFDDRVTGNISKFAPEA
KLAASEGRGGILHFEISPKNINKVVEATEAIEGDVTANLQSFIPLVDSIE
NRPEWFNKINEWKKKYPYSYQLETPGSLIKPQTLIKEISDQAQTYNKEVI
VTTGVGQHQMWAAQHFTWTQPRTMITSGGLGTMGYGLPAAIGAQVAKPDA
IVIDIDGDASFNMTLTELSSAVQAGAPIKVCVLNNEEQGMVTQWQSLFYE
HRYSHTHQSNPDFMKLAESMNVKGIRITNQQELKSGVKEFLDATEPVLLE
VIVEKKVPVLPMVPAGKALDDFILWDAEVEKQQNDLRKERTGGKY

3D structure

PDB

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

Chain

Resolution

2.971 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 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)	Y34 G36 G37 A38 I39 E60 T83 Q118 E119 K167 K226 M262 V289 V405 L430 G431 M433 D458 N485 E487 Q488 M490 V491 W494 L516 N521 V522
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 M350 G370 A371 R372 D374 R376 V377 E403 I404 N408 D422 V423 M498 G516	R157 G215 A216 G217 N220 T242 L243 Q244 L260 M262 G282 A283 R284 D286 R288 V289 E315 I316 N320 D334 V335 M410 G428
BS02	MG	A	D546 N573 E575	D458 N485 E487
BS03	TPP	A	V493 G494 Q495 H496 M521 G545 D546 A547 S548 N573 E575 Q576 G577 M578 V579	V405 G406 Q407 H408 M433 G457 D458 A459 S460 N485 E487 Q488 G489 M490 V491

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

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