Structure of PDB 6bd9 Chain B Binding Site BS08

Receptor Information

>6bd9 Chain B (length=564) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

PDMDTSFVGLTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFN
FVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTPMADAFADGI
PMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINE
AFEIATSGRPGPVLVDLPKDVTAAILRNPIPTKTTLPSNALNQLTSRAQD
EFVMQSINKAADLINLAKKPVLYVGAGILNHADGPRLLKELSDRAQIPVT
TTLQGLGSFDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVT
GNISKFAPEARRAAAEGRGGIIHFEVSPKNINKVVQTQIAVEGDATTNLG
KMMSKIFPVKERSEWFAQINKWKKEYPYAYMEETPGSKIKPQTVIKKLSK
VANDTGRHVIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAA
IGAQVAKPESLVIDIDGDASFNMTLTELSSAVQAGTPVKILILNNEEQGM
VTQWQSLFYEHRYSHTHQLNPDFIKLAEAMGLKGLRVKKQEELDAKLKEF
VSTKGPVLLEVEVD

Ligand information

InChI=1S/O2/c1-2

MYMOFIZGZYHOMD-UHFFFAOYSA-N

SMILES

Software	SMILES
CACTVS 3.341 OpenEye OEToolkits 1.5.0	O=O

Formula

Name

OXYGEN MOLECULE

PDB chain

6bd9 Chain B Residue 710 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

Global view

Local view

Structure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]

PDB	6bd9 High resolution crystal structures of the acetohydroxyacid synthase-pyruvate complex provide new insights into its catalytic mechanism
Resolution	1.982 Å
Binding residue (original residue number in PDB)	G116 A117 T162 Q202
Binding residue (residue number reindexed from 1)	G34 A35 T80 Q120
Annotation score	1

Enzymatic activity

Catalytic site (original residue number in PDB)	Y113 G115 G116 A117 I118 E139 T162 F201 Q202 E203 K251 R318 M354 V381 V497 L522 G523 M525 D550 N577 E579 Q580 M582 V583 W586 L608 G613 L614
Catalytic site (residue number reindexed from 1)	Y31 G33 G34 A35 I36 E57 T80 F119 Q120 E121 K169 R236 M272 V299 V415 L440 G441 M443 D468 N495 E497 Q498 M500 V501 W504 L526 G531 L532
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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component

External links

PDB	RCSB:6bd9, PDBe:6bd9, PDBj:6bd9
PDBsum	6bd9
PubMed
UniProt	P07342\|ILVB_YEAST Acetolactate synthase catalytic subunit, mitochondrial (Gene Name=ILV2)

[Back to BioLiP]