Structure of PDB 1ozg Chain A

Receptor sequence

>1ozgA (length=549) Species: 573 (Klebsiella pneumoniae)

PVRQWAHGADLVVSQLEAQGVRQVFGIPGAKIDKVFDSLLDSSIRIIPVR
HEANAAFMAAAVGRITGKAGVALVTSGPGCSNLITGMATANSEGDPVVAL
GGAVKRADKAKQVHQSMDTVAMFSPVTKYAIEVTAPDALAEVVSNAFRAA
EQGRPGSAFVSLPQDVVDGPVSGKVLPASGAPQMGAAPDDAIDQVAKLIA
QAKNPIFLLGLMASQPENSKALRRLLETSHIPVTSTYQAAGAVNQDNFSR
FAGRVGLFNNQAGDRLLQLADLVICIGYSPVEYEPAMWNSGNATLVHIDV
LPAYEERNYTPDVELVGDIAGTLNKLAQNIDHRLVLSPQAAEILRDRQHQ
RELLDRRGAQLNQFALHPLRIVRAMQDIVNSDVTLTVDMGSFHIWIARYL
YTFRARQVMISNGQQTMGVALPWAIGAWLVNPERKVVSVSGDGGFLQSSM
ELETAVRLKANVLHLIWVDNGYNMVAIQEEKKYQRLSGVEFGPMDFKAYA
ESFGAKGFAVESAEALEPTLRAAMDVDGPAVVAIPVDYRDNPLLMGQLH

3D structure

• PDB: 1ozg 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): I27 G29 A30 K31 I32 E52 T75 H114 Q115 S116 Q164 L257 E284 M389 Q415 M417 D442 D469 G471 Y472 M474 V475 Q478 Y538
• 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 Y406	G253 R254 Q261 R347 R398 Y401
BS02	MG	A	D447 D474 G476	D442 D469 G471
BS03	HE3	A	M394 G395 S396 F397 Q420 M422 G446 D447 G448 D474 G476 Y477 N478 M479 V480 Y543	M389 G390 S391 F392 Q415 M417 G441 D442 G443 D469 G471 Y472 N473 M474 V475 Y538

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