Structure of PDB 1jsc Chain B

Receptor sequence

>1jscB (length=550) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]

EPDMDTSFVGLTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKF
NFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTPMADAFADG
IPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRIN
EAFEIATSGRPGPVLVDLPKDVTAAILRNPIPTKTTLPSNALTSRAQDEF
VMQSINKAADLINLAKPVLYVGAGILNHADGPRLLKELSDRAQIPVTTTL
QGLGSFDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVTGNI
SKFAPEARRAAIIHFEVSPKNINKVVQTQIAVEGDATTNLGKMMSKIFPV
RSEWFAQINKWKKEYEETPGSKIKPQTVIKKLSKVANDTGRHVIVTTGVG
QHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDID
GDASFNMTLTELSSAVQAGTPVKILILNNEEQGMVTQWQSLFEHRYSHTH
QLNPDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGPVLLEVEVDKKV

3D structure

PDB

1jsc Crystal structure of yeast acetohydroxyacid synthase: a target for herbicidal inhibitors.

Chain

Resolution

2.6 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	Y113 G115 G116 A117 I118 E139 T162 F201 Q202 E203 K251 M354 V381 V497 G523 M525 D550 N577 E579 Q580 M582 V583 W586 K647
Catalytic site (residue number reindexed from 1)	Y32 G34 G35 A36 I37 E58 T81 F120 Q121 E122 K170 M269 V296 V399 G425 M427 D452 N479 E481 Q482 M484 V485 W488 K548
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	TPP	B	Y113 P114 E139 P165	Y32 P33 E58 P84
BS02	MG	B	D550 N577	D452 N479
BS03	2HP	B	T598 H599	T499 H500
BS04	2HP	B	G116 Q202	G35 Q121
BS05	TPP	B	V497 G498 Q499 H500 M525 D550 A551 S552 N577	V399 G400 Q401 H402 M427 D452 A453 S454 N479
BS06	FAD	B	R241 G307 A308 G309 N312 T334 L335 M351 L352 G353 H355 G374 A375 R376 D378 R380 V381 E407 V408 N412 D426 A427 M502 G520	R160 G222 A223 G224 N227 T249 L250 M266 L267 G268 H270 G289 A290 R291 D293 R295 V296 E316 V317 N321 D335 A336 M404 G422

Gene Ontology

	Molecular Function
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:0008652	amino acid biosynthetic process
GO:0009082	branched-chain amino acid biosynthetic process
GO:0009097	isoleucine biosynthetic process
GO:0009099	L-valine biosynthetic process

	Cellular Component
GO:0005739	mitochondrion
GO:0005948	acetolactate synthase complex

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component

External links

PDB	RCSB:1jsc, PDBe:1jsc, PDBj:1jsc
PDBsum	1jsc
PubMed	11902841
UniProt	P07342\|ILVB_YEAST Acetolactate synthase catalytic subunit, mitochondrial (Gene Name=ILV2)

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