Structure of PDB 6dem Chain A

Receptor sequence

>6demA (length=597) Species: 237561 (Candida albicans SC5314) [Search protein sequence]

KEQLMDDSFIGLTGGEIFHEMMLRHKVDTVFGYAGGAILPVFDAIYNSDK
FKFVLPRHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVITPMADALMD
GVPLVVFSGQVPTTAIGTDAFQEADIVGISRSCTKWNVMVKNVAELPRRI
NEAFEIATTGRPGPVLVDLPKDVTASILRESIPINTTLPSVSEFTSEAIK
RAANILNKAKKPIIYAGAGILNNEQGPKLLKELADKANIPVTTTLQGLGA
FDQRDPKSLDMLGMHGSAAANTAIQNADCIIALGARFDDRVTGNISKFAP
EAKLAASEGRGGILHFEISPKNINKVVEATEAIEGDVTANLQSFIPLVDS
IENRPEWFNKINEWKKKYPYSYQLETPGSLIKPQTLIKEISDQAQTYNKE
VIVTTGVGQHQMWAAQHFTWTQPRTMITSGGLGTMGYGLPAAIGAQVAKP
DAIVIDIDGDASFNMTLTELSSAVQAGAPIKVCVLNNEEQGMVTQWQSLF
YEHRYSHTHQSNPDFMKLAESMNVKGIRITNQQELKSGVKEFLDATEPVL
LEVIVEKKVPVLPMVPAGKALDDFILWDAEVEKQQNDLRKERTGGKY

3D structure

PDB

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

Chain

Resolution

2.038 Å

3D
structure

Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]

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 K228 M264 V291 V407 L432 G433 M435 D460 N487 E489 Q490 M492 V493 W496 L518 N523 V524
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 N408 D422 V423 M498 G516	R161 G217 A218 G219 N222 T244 L245 Q246 L262 G284 A285 R286 D288 R290 V291 E317 I318 N322 D336 V337 M412 G430
BS02	MG	A	D546 N573 E575	D460 N487 E489
BS03	TP9	A	V493 G494 Q495 H496 M521 G545 D546 A547 S548 M551 N573 E575 Q576 G577 M578 V579	V407 G408 Q409 H410 M435 G459 D460 A461 S462 M465 N487 E489 Q490 G491 M492 V493
BS04	60G	A	M350 D375 R376 M578 W582 A653	M264 D289 R290 M492 W496 A567

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

[Back to BioLiP]