Structure of PDB 1ozf Chain B Binding Site BS02

Receptor Information
>1ozf Chain B (length=542) Species: 573 (Klebsiella pneumoniae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
YPVRQWAHGADLVVSQLEAQGVRQVFGIPGAKIDKVFDSLLDSSIRIIPV
RHEANAAFMAAAVGRITGKAGVALVTSGPGCSNLITGMATANSEGDPVVA
LGGAVKRADKAKQSMDTVAMFSPVTKYAIEVTAPDALAEVVSNAFRAAEQ
GRPGSAFVSLPQDVVDGPVSGKVLPAPQMGAAPDDAIDQVAKLIAQAKNP
IFLLGLMASQPENSKALRRLLETSHIPVTSTYQAAGAVNQDNFSRFAGRV
GLFNNQAGDRLLQLADLVICIGYSPVEYEPAMWNSGNATLVHIDVLPAYE
ERNYTPDVELVGDIAGTLNKLAQNIDHRLVLSPQAAEILRDRQHQRELLD
RAQLNQFALHPLRIVRAMQDIVNSDVTLTVDMGSFHIWIARYLYTFRARQ
VMISNGQQTMGVALPWAIGAWLVNPERKVVSVSGDGGFLQSSMELETAVR
LKANVLHLIWVDNGYNMVAIQEEKKYQRLSGVEFGPMDFKAYAESFGAKG
FAVESAEALEPTLRAAMDVDGPAVVAIPVDYRDNPLLMGQLH
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain1ozf Chain B Residue 704 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1ozf The Crystal Structures of Klebsiella pneumoniae Acetolactate Synthase with Enzyme-bound Cofactor and with an Unusual Intermediate.
Resolution2.3 Å
Binding residue
(original residue number in PDB)		D447 D474 G476
Binding residue
(residue number reindexed from 1)		D435 D462 G464
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) I32 G34 A35 K36 I37 E57 T80 S121 Q169 L262 E289 M394 Q420 M422 D447 D474 G476 Y477 M479 V480 Q483 Y543
Catalytic site (residue number reindexed from 1) I28 G30 A31 K32 I33 E53 T76 S114 Q162 L252 E279 M382 Q408 M410 D435 D462 G464 Y465 M467 V468 Q471 Y531
Enzyme Commision number 2.2.1.6: acetolactate synthase.
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1ozf, PDBe:1ozf, PDBj:1ozf
PDBsum1ozf
PubMed14557277
UniProtP27696|ILVB_KLEPN Acetolactate synthase, catabolic (Gene Name=budB)

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