Structure of PDB 1ozh Chain D Binding Site BS02

Receptor Information
>1ozh Chain D (length=538) Species: 573 (Klebsiella pneumoniae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VRQWAHGADLVVSQLEAQGVRQVFGIPGAKIDKVFDSLLDSSIRIIPVRH
EANAAFMAAAVGRITGKAGVALVTSGPGCSNLITGMATANSEGDPVVALG
GAVKRADKSMDTVAMFSPVTKYAIEVTAPDALAEVVSNAFRAAEQGRPGS
AFVSLPQDVVDGPVSGKVLPASGAPQMGAAPDDAIDQVAKLIAQAKNPIF
LLGLMASQPENSKALRRLLETSHIPVTSTYQAAGAVNQDNFSRFAGRVGL
FNNQAGDRLLQLADLVICIGYSPVEYEPAMWNSGNATLVHIDVLPAYEER
NYTPDVELVGDIAGTLNKLAQNIDHRLVLSPQAAEILRDRQHQRELLDLN
QFALHPLRIVRAMQDIVNSDVTLTVDMGSFHIWIARYLYTFRARQVMISN
GQQTMGVALPWAIGAWLVNPERKVVSVSGDGGFLQSSMELETAVRLKANV
LHLIWVDNGYNMVAIQEEKKYQRLSGVEFGPMDFKAYAESFGAKGFAVES
AEALEPTLRAAMDVDGPAVVAIPVDYRDNPLLMGQLHL
Ligand information
Ligand IDPO4
InChIInChI=1S/H3O4P/c1-5(2,3)4/h(H3,1,2,3,4)/p-3
InChIKeyNBIIXXVUZAFLBC-UHFFFAOYSA-K
SMILES
SoftwareSMILES
CACTVS 3.341[O-][P]([O-])([O-])=O
ACDLabs 10.04[O-]P([O-])([O-])=O
OpenEye OEToolkits 1.5.0[O-]P(=O)([O-])[O-]
FormulaO4 P
NamePHOSPHATE ION
ChEMBL
DrugBankDB14523
ZINC
PDB chain1ozh Chain D Residue 1431 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1ozh The Crystal Structures of Klebsiella pneumoniae Acetolactate Synthase with Enzyme-bound Cofactor and with an Unusual Intermediate.
Resolution2.0 Å
Binding residue
(original residue number in PDB)		G258 R259 Q266 R352 Y406
Binding residue
(residue number reindexed from 1)		G246 R247 Q254 R340 Y389
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) I26 G28 A29 K30 I31 E51 T74 S109 Q157 L250 E277 M377 Q403 M405 D430 D457 G459 Y460 M462 V463 Q466 Y526
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:1ozh, PDBe:1ozh, PDBj:1ozh
PDBsum1ozh
PubMed14557277
UniProtP27696|ILVB_KLEPN Acetolactate synthase, catabolic (Gene Name=budB)

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