Structure of PDB 6dep Chain A

Receptor sequence

>6depA (length=598) Species: 237561 (Candida albicans SC5314) [Search protein sequence]

KEQLMDDSFIGLTGGEIFHEMMLRHKVDTVFGYAGGAILPVFDAIYNSDK
FKFVLPRHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVITPMADALMD
GVPLVVFSGQVPTTAIGTDAFQEADIVGISRSCTKWNVMVKNVAELPRRI
NEAFEIATTGRPGPVLVDLPKDVTASILRESIPINTTLPSAVSEFTSEAI
KRAANILNKAKKPIIYAGAGILNNEQGPKLLKELADKANIPVTTTLQGLG
AFDQRDPKSLDMLGMHGSAAANTAIQNADCIIALGARFDDRVTGNISKFA
PEAKLAASEGRGGILHFEISPKNINKVVEATEAIEGDVTANLQSFIPLVD
SIENRPEWFNKINEWKKKYPYSYQLETPGSLIKPQTLIKEISDQAQTYNK
EVIVTTGVGQHQMWAAQHFTWTQPRTMITSGGLGTMGYGLPAAIGAQVAK
PDAIVIDIDGDASFNMTLTELSSAVQAGAPIKVCVLNNEEQGMVTQWQSL
FYEHRYSHTHQSNPDFMKLAESMNVKGIRITNQQELKSGVKEFLDATEPV
LLEVIVEKKVPVLPMVPAGKALDDFILWDAEVEKQQNDLRKERTGGKY

3D structure

PDB

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

Chain

Resolution

2.149 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)	Y33 G35 G36 A37 I38 E59 T82 F121 Q122 E123 K171 K229 M265 V292 V408 L433 G434 M436 D461 N488 E490 Q491 M493 V494 W497 L519 N524 V525
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 G349 G370 A371 R372 D374 R376 V377 E403 I404 N408 D422 V423 M498 G516	R161 G218 A219 G220 N223 T245 L246 Q247 L263 G264 G285 A286 R287 D289 R291 V292 E318 I319 N323 D337 V338 M413 G431
BS02	MG	A	D546 N573 E575	D461 N488 E490
BS03	1SM	A	D375 R376 M578 W582	D290 R291 M493 W497
BS04	TZD	A	V493 G494 Q495 H496 G519 M521 G545 D546 A547 S548 M551 N573 E575 Q576 G577 M578 V579	V408 G409 Q410 H411 G434 M436 G460 D461 A462 S463 M466 N488 E490 Q491 G492 M493 V494
BS05	TP9	A	V493 G494 Q495 H496 G519 M521 G545 D546 A547 S548 M551 N573 E575 Q576 G577 M578 V579	V408 G409 Q410 H411 G434 M436 G460 D461 A462 S463 M466 N488 E490 Q491 G492 M493 V494

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

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