Structure of PDB 3iaf Chain C

Receptor sequence

>3iafC (length=554) Species: 294 (Pseudomonas fluorescens) [Search protein sequence]

AMITGGELVVRTLIKAGVEHLFGLHGSHIDTIFQACLDHDVPIIDTRHEA
AAGHAAEGYARAGAKLGVALVTAGGGFTNAVTPIANAWLDRTPVLFLTGS
GALRDDETNTLQAGIDQVAMAAPITKWAHRVMATEHIPRLVMQAIRAALS
APRGPVLLDLPWDILMNQIDEDSVIIPDLVLSAHGARPDPADLDQALALL
RKAERPVIVLGSEASRTARKTALSAFVAATGVPVFADYEGLSMLSGLPDA
MRGGLVQNLYSFAKADAAPDLVLMLGARFGLNTGHGSGQLIPHSAQVIQV
DPDACELGRLQGIALGIVADVGGTIEALAQATAQDAAWPDRGDWCAKVTD
LAQERYASIAAKSSSEHALHPFHASQVIAKHVDAGVTVVADGALTYLWLS
EVMSRVKPGGFLCHGYLGSMGVGFGTALGAQVADLEAGRRTILVTGDGSV
GYSIGEFDTLVRKQLPLIVIIMNNQSWGATLHFQQLAVGPNRVTGTRLEN
GSYHGVAAAFGADGYHVDSVESFSAALAQALAHNRPACINVAVALDPIPP
EELI

3D structure

PDB

3iaf Active-site engineering of benzaldehyde lyase shows that a point mutation can confer both new reactivity and susceptibility to mechanism-based inhibition.

Chain

Resolution

2.8 Å

3D
structure

Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]

Enzymatic activity

Catalytic site (original residue number in PDB)	L25 G27 S28 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)	L24 G26 S27 H28 I29 E49 T72 L111 Q112 A113 G114 W162 L255 T283 G392 G418 M420 D447 N474 S476 W477 A479 T480 F483 L545
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	C	G393 A394 L395 T396 G419 S420 M421 G449 S450 Y453 N475 S477 W478 G479 T481	G392 A393 L394 T395 G418 S419 M420 G448 S449 Y452 N474 S476 W477 G478 T480
BS02	MG	C	D448 N475 S477	D447 N474 S476
BS03	TPP	C	H26 S28 E50 T73 G76	H25 S27 E49 T72 G75

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

View graph for
Biological Process

View graph for
Cellular Component

External links

PDB	RCSB:3iaf, PDBe:3iaf, PDBj:3iaf
PDBsum	3iaf
PubMed	20030408
UniProt	Q9F4L3

[Back to BioLiP]