Structure of PDB 6u9d Chain B Binding Site BS03

Receptor Information

>6u9d Chain B (length=607) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

AEPDMDTSFVGLTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDK
FNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTPMADAFAD
GIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRI
NEAFEIATSGRPGPVLVDLPKDVTAAILRNPIPTKTTLPSNALNQLTSRA
QDEFVMQSINKAADLINLAKKPVLYVGAGILNHADGPRLLKELSDRAQIP
VTTTLQGLGSFDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDR
VTGNISKFAPEARRAAAEGRGGIIHFEVSPKNINKVVQTQIAVEGDATTN
LGKMMSKIFPVKERSEWFAQINKWKKEYPYAYMEETPGSKIKPQTVIKKL
SKVANDTGRHVIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLP
AAIGAQVAKPESLVIDIDGDASFNMTLTELSSAVQAGTPVKILILNNEEQ
GMVTQWQSLFYEHRYSHTHQLNPDFIKLAEAMGLKGLRVKKQEELDAKLK
EFVSTKGPVLLEVEVDKKVPVLPMVAGGSGLDEFINFDPEVERQQTELRH
KRTGGKH

Ligand information

Ligand ID

TPP

InChI

InChI=1S/C12H18N4O7P2S/c1-8-11(3-4-22-25(20,21)23-24(17,18)19)26-7-16(8)6-10-5-14-9(2)15-12(10)13/h5,7H,3-4,6H2,1-2H3,(H4-,13,14,15,17,18,19,20,21)/p+1

InChIKey

AYEKOFBPNLCAJY-UHFFFAOYSA-O

SMILES

Software	SMILES
CACTVS 3.341	Cc1ncc(C[n+]2csc(CCO[P@@](O)(=O)O[P](O)(O)=O)c2C)c(N)n1
OpenEye OEToolkits 1.5.0	Cc1c(sc[n+]1Cc2cnc(nc2N)C)CCO[P@](=O)(O)OP(=O)(O)O
OpenEye OEToolkits 1.5.0	Cc1c(sc[n+]1Cc2cnc(nc2N)C)CCOP(=O)(O)OP(=O)(O)O
CACTVS 3.341	Cc1ncc(C[n+]2csc(CCO[P](O)(=O)O[P](O)(O)=O)c2C)c(N)n1
ACDLabs 10.04	O=P(O)(O)OP(=O)(O)OCCc1sc[n+](c1C)Cc2c(nc(nc2)C)N

Formula

C12 H19 N4 O7 P2 S

Name

THIAMINE DIPHOSPHATE

PDB chain

6u9d Chain B Residue 701 [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)	V497 G498 Q499 H500 G523 M525 A551 S552 N577 E579 Q580 G581 M582 V583
Binding residue (residue number reindexed from 1)	V417 G418 Q419 H420 G443 M445 A471 S472 N497 E499 Q500 G501 M502 V503
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)	Y33 G35 G36 A37 I38 E59 T82 F121 Q122 E123 K171 M274 V301 V417 G443 M445 D470 N497 E499 Q500 M502 V503 W506
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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