Structure of PDB 4qpz Chain F Binding Site BS02

Receptor Information

>4qpz Chain F (length=562) Species: 294 (Pseudomonas fluorescens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

AMITGGELVVRTLIKAGVEHLFGLHGIHIDTIFQACLDHDVPIIDTRHEA
AAGHAAEGYARAGAKLGVALVTAGGGFTNAVTPIANAWLDRTPVLFLTGS
GALRDDETNTLQAGIDQVAMAAPITKWAHRVMATEHIPRLVMQAIRAALS
APRGPVLLDLPWDILMNQIDEDSVIIPDLVLSAHGARPDPADLDQALALL
RKAERPVIVLGSEASRTARKTALSAFVAATGVPVFADYEGLSMLSGLPDA
MRGGLVQNLYSFAKADAAPDLVLMLGARFGLNTGHGSGQLIPHSAQVIQV
DPDACELGRLQGIALGIVADVGGTIEALAQATAQDAAWPDRGDWCAKVTD
LAQERYASIAAKSSSEHALHPFHASQVIAKHVDAGVTVVADGGLTYLWLS
EVMSRVKPGGFLCHGYLNSMGVGFGTALGAQVADLEAGRRTILVTGDGSV
GYSIGEFDTLVRKQLPLIVIIMNNQSWGWTLHFQQLAVGPNRVTGTRLEN
GSYHGVAAAFGADGYHVDSVESFSAALAQALAHNRPACINVAVALDPIPP
EELILIGMDPFA

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

4qpz Chain F Residue 601 [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	4qpz Computational protein design enables a novel one-carbon assimilation pathway.
Resolution	3.0 Å
Binding residue (original residue number in PDB)	D448 N475
Binding residue (residue number reindexed from 1)	D447 N474
Annotation score	1

Enzymatic activity

Catalytic site (original residue number in PDB)	L25 G27 I28 H29 I30 E50 T73 L112 Q113 A114 G115 W163 L256 T284 G393 N419 M421 D448 N475 S477 W478 W480 T481 F484 L546
Catalytic site (residue number reindexed from 1)	L24 G26 I27 H28 I29 E49 T72 L111 Q112 A113 G114 W162 L255 T283 G392 N418 M420 D447 N474 S476 W477 W479 T480 F483 L545
Enzyme Commision number	?

Gene Ontology

	Molecular Function
GO:0000287	magnesium ion binding
GO:0003824	catalytic activity
GO:0003984	acetolactate synthase activity
GO:0016829	lyase activity
GO:0030976	thiamine pyrophosphate binding
GO:0046872	metal ion binding
GO:0050660	flavin adenine dinucleotide binding

	Biological Process
GO:0009097	isoleucine biosynthetic process
GO:0009099	L-valine biosynthetic process
GO:0019752	carboxylic acid metabolic process

	Cellular Component
GO:0005948	acetolactate synthase complex

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Cellular Component

External links

PDB	RCSB:4qpz, PDBe:4qpz, PDBj:4qpz
PDBsum	4qpz
PubMed	25775555
UniProt	Q9F4L3

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