Structure of PDB 1ozf Chain A

Receptor sequence

>1ozfA (length=545) Species: 573 (Klebsiella pneumoniae)

VRQWAHGADLVVSQLEAQGVRQVFGIPGAKIDKVFDSLLDSSIRIIPVRH
EANAAFMAAAVGRITGKAGVALVTSGPGCSNLITGMATANSEGDPVVALG
GAVKRADKAKQVHQSMDTVAMFSPVTKYAIEVTAPDALAEVVSNAFRAAE
QGRPGSAFVSLPQDVVDGPVSGKVLPAPQMGAAPDDAIDQVAKLIAQAKN
PIFLLGLMASQPENSKALRRLLETSHIPVTSTYQAAGAVNQDNFSRFAGR
VGLFNNQAGDRLLQLADLVICIGYSPVEYEPAMWNSGNATLVHIDVLPAY
EERNYTPDVELVGDIAGTLNKLAQNIDHRLVLSPQAAEILRDRQHQRELL
DRRGAQLNQFALHPLRIVRAMQDIVNSDVTLTVDMGSFHIWIARYLYTFR
ARQVMISNGQQTMGVALPWAIGAWLVNPERKVVSVSGDGGFLQSSMELET
AVRLKANVLHLIWVDNGYNMVAIQEEKKYQRLSGVEFGPMDFKAYAESFG
AKGFAVESAEALEPTLRAAMDVDGPAVVAIPVDYRDNPLLMGQLH

3D structure

• PDB: 1ozf The Crystal Structures of Klebsiella pneumoniae Acetolactate Synthase with Enzyme-bound Cofactor and with an Unusual Intermediate.
• Chain: A
• Resolution: 2.3 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): I32 G34 A35 K36 I37 E57 T80 H119 Q120 S121 Q169 L262 E289 M394 Q420 M422 D447 D474 G476 Y477 M479 V480 Q483 Y543
• Catalytic site (residue number reindexed from 1): I26 G28 A29 K30 I31 E51 T74 H113 Q114 S115 Q163 L253 E280 M385 Q411 M413 D438 D465 G467 Y468 M470 V471 Q474 Y534
• Enzyme Commision number: 2.2.1.6: acetolactate synthase.

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)	Binding affinity
BS01	PO4	A	G258 R259 Q266 R352 R403 L405 Y406	G249 R250 Q257 R343 R394 L396 Y397
BS02	MG	A	D447 D474 G476	D438 D465 G467
BS03	TPP	A	G395 S396 F397 Q420 M422 G446 D447 G448 D474 G476 Y477 N478 M479 V480 Y543	G386 S387 F388 Q411 M413 G437 D438 G439 D465 G467 Y468 N469 M470 V471 Y534

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:0009097 isoleucine biosynthetic process
• GO:0009099 L-valine biosynthetic process
• GO:0019752 carboxylic acid metabolic process
• GO:0034077 butanediol metabolic process

Cellular Component

• GO:0005948 acetolactate synthase complex

External links

• PDB: RCSB:1ozf, PDBe:1ozf, PDBj:1ozf
• PDBsum: 1ozf
• PubMed: 14557277
• UniProt: P27696|ILVB_KLEPN Acetolactate synthase, catabolic (Gene Name=budB)