Structure of PDB 4qpz Chain H

Receptor sequence

>4qpzH (length=562) Species: 294 (Pseudomonas fluorescens) [Search protein sequence]

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

3D structure

PDB

4qpz Computational protein design enables a novel one-carbon assimilation pathway.

Chain

Resolution

3.0 Å

3D
structure

Catalytic site residues are labeled in the structure
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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	?

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)
BS01	TPP	H	T73 G76	T72 G75
BS02	MG	H	D448 N475 S477	D447 N474 S476
BS03	TPP	H	G393 G394 L395 N419 S420 M421 G447 D448 G449 S450 Y453 N475 S477 W478 G479 W480 T481	G392 G393 L394 N418 S419 M420 G446 D447 G448 S449 Y452 N474 S476 W477 G478 W479 T480

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

View graph for
Molecular Function

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Biological Process

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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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