Structure of PDB 6u9d Chain N Binding Site BS02

Receptor Information

>6u9d Chain N (length=603) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

MDTSFVGLTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFNFV
LPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTPMADAFADGIPM
VVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAF
EIATSGRPGPVLVDLPKDVTAAILRNPIPTKTTLPSNALNQLTSRAQDEF
VMQSINKAADLINLAKKPVLYVGAGILNHADGPRLLKELSDRAQIPVTTT
LQGLGSFDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVTGN
ISKFAPEARRAAAEGRGGIIHFEVSPKNINKVVQTQIAVEGDATTNLGKM
MSKIFPVKERSEWFAQINKWKKEYPYAYMEETPGSKIKPQTVIKKLSKVA
NDTGRHVIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIG
AQVAKPESLVIDIDGDASFNMTLTELSSAVQAGTPVKILILNNEEQGMVT
QWQSLFYEHRYSHTHQLNPDFIKLAEAMGLKGLRVKKQEELDAKLKEFVS
TKGPVLLEVEVDKKVPVLPMVAGGSGLDEFINFDPEVERQQTELRHKRTG
GKH

Ligand information

Ligand ID

InChI

InChI=1S/Mg/q+2

InChIKey

JLVVSXFLKOJNIY-UHFFFAOYSA-N

SMILES

Software	SMILES
ACDLabs 10.04 OpenEye OEToolkits 1.5.0	[Mg+2]
CACTVS 3.341	[Mg++]

Formula

Name

MAGNESIUM ION

PDB chain

6u9d Chain N Residue 702 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

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Structure summary

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PDB	6u9d Structures of fungal and plant acetohydroxyacid synthases.
Resolution	3.194 Å
Binding residue (original residue number in PDB)	D550 N577 E579
Binding residue (residue number reindexed from 1)	D466 N493 E495
Annotation score	1

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)	Y29 G31 G32 A33 I34 E55 T78 F117 Q118 E119 K167 M270 V297 V413 G439 M441 D466 N493 E495 Q496 M498 V499 W502
Enzyme Commision number	2.2.1.6: acetolactate synthase.

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

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Molecular Function

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Biological Process

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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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