Structure of PDB 2ag1 Chain D

Receptor sequence

>2ag1D (length=553) Species: 294 (Pseudomonas fluorescens) [Search protein sequence]

MITGGELVVRTLIKAGVEHLFGLHGAHIDTIFQACLDHDVPIIDTRHEAA
AGHAAEGYARAGAKLGVALVTAGGGFTNAVTPIANAWLDRTPVLFLTGSG
ALRDDETNTLQAGIDQVAMAAPITKWAHRVMATEHIPRLVMQAIRAALSA
PRGPVLLDLPWDILMNQIDEDSVIIPDLVLSAHGARPDPADLDQALALLR
KAERPVIVLGSEASRTARKTALSAFVAATGVPVFADYEGLSMLSGLPDAM
RGGLVQNLYSFAKADAAPDLVLMLGARFGLNTGHGSGQLIPHSAQVIQVD
PDACELGRLQGIALGIVADVGGTIEALAQATAQDAAWPDRGDWCAKVTDL
AQERYASIAAKSSSEHALHPFHASQVIAKHVDAGVTVVADGALTYLWLSE
VMSRVKPGGFLCHGYLGSMGVGFGTALGAQVADLEAGRRTILVTGDGSVG
YSIGEFDTLVRKQLPLIVIIMNNQSWGATLHFQQLAVGPNRVTGTRLENG
SYHGVAAAFGADGYHVDSVESFSAALAQALAHNRPACINVAVALDPIPPE
ELI

3D structure

PDB

2ag1 Structure and mechanism of the ThDP-dependent benzaldehyde lyase from Pseudomonas fluorescens

Chain

Resolution

2.58 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 A28 H29 I30 E50 T73 L112 Q113 A114 G115 W163 L256 T284 G393 G419 M421 D448 N475 S477 W478 A480 T481 F484 L546
Catalytic site (residue number reindexed from 1)	L23 G25 A26 H27 I28 E48 T71 L110 Q111 A112 G113 W161 L254 T282 G391 G417 M419 D446 N473 S475 W476 A478 T479 F482 L544
Enzyme Commision number	4.1.2.38: benzoin aldolase.

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	D	H26 E50 T73 Q113	H24 E48 T71 Q111
BS02	MG	D	D448 N475 S477	D446 N473 S475
BS03	TPP	D	G393 A394 L395 T396 G419 S420 M421 G447 D448 G449 S450 Y453 N475 S477 W478 G479	G391 A392 L393 T394 G417 S418 M419 G445 D446 G447 S448 Y451 N473 S475 W476 G477

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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Molecular Function

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Biological Process

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Cellular Component

External links

PDB	RCSB:2ag1, PDBe:2ag1, PDBj:2ag1
PDBsum	2ag1
PubMed	16302970
UniProt	Q9F4L3

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