Structure of PDB 6u9d Chain J

Receptor sequence

>6u9dJ (length=602) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]

DMDTSFVGLTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFNF
VLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTPMADAFADGIP
MVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEA
FEIATSGRPGPVLVDLPKDVTAAILRNPIPTKTTLPSNALNQLTSRAQDE
FVMQSINKAADLINLAKKPVLYVGAGILNHADGPRLLKELSDRAQIPVTT
TLQGLGSFDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVTG
NISKFAPEARRAAAEGRGGIIHFEVSPKNINKVVQTQIAVEGDATTNLGK
MMSKIFPVKERSEWFAQINKWKKEYPYAYMEETPGSKIKPQTVIKKLSKV
ANDTGRHVIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAI
GAQVAKPESLVIDIDGDASFNMTLTELSSAVQAGTPVKILILNNEEQGMV
TQWQSLFYEHRYSHTHQLNPDFIKLAEAMGLKGLRVKKQEELDAKLKEFV
STKGPVLLEVEVDKKVPVLPMVAGGSGLDEFINFDPEVERQQTELRHKRT
GG

3D structure

PDB

6u9d Structures of fungal and plant acetohydroxyacid synthases.

Chain

Resolution

3.194 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
Catalytic site (residue number reindexed from 1)	Y30 G32 G33 A34 I35 E56 T79 F118 Q119 E120 K168 M271 V298 V414 G440 M442 D467 N494 E496 Q497 M499 V500 W503
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)	Binding affinity
BS01	TPP	J	P114 E139 P165	P31 E56 P82
BS02	60G	J	G116 A117 V191 P192 F201 K251	G33 A34 V108 P109 F118 K168	BindingDB: Ki=4.4nM
BS03	TPP	J	V497 Q499 H500 G523 M525 D550 A551 S552 M555 N577 E579 Q580 G581 M582 V583	V414 Q416 H417 G440 M442 D467 A468 S469 M472 N494 E496 Q497 G498 M499 V500
BS04	MG	J	D550 N577 E579	D467 N494 E496
BS05	FAD	J	R241 G307 G309 N312 T334 L335 L352 G353 M354 G374 R376 D378 R380 V381 E407 V408 N412 D426 A427 M502 G520 G521	R158 G224 G226 N229 T251 L252 L269 G270 M271 G291 R293 D295 R297 V298 E324 V325 N329 D343 A344 M419 G437 G438
BS06	60G	J	D379 R380 M582 W586	D296 R297 M499 W503	BindingDB: Ki=4.4nM

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:6u9d, PDBe:6u9d, PDBj:6u9d
PDBsum	6u9d
PubMed	32640464
UniProt	P07342\|ILVB_YEAST Acetolactate synthase catalytic subunit, mitochondrial (Gene Name=ILV2)

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