Structure of PDB 1szo Chain K Binding Site BS01

Receptor Information
>1szo Chain K (length=249) Species: 157732 (Rhodococcus sp. NCIMB 9784) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
LATPFQEYSQKYENIRLERDGGVLLVTVHTEGKSLVWTSTAHDELAYCFH
DIACDRENKVVILTGTGPSFCNEIDFTSFNLGTPHDWDEIIFEGQRLLNN
LLSIEVPVIAAVNGPVTNAPEIPVMSDIVLAAESATFQDGPHFPSGIVPG
DGAHVVWPHVLGSNRGRYFLLTGQELDARTALDYGAVNEVLSEQELLPRA
WELARGIAEKPLLARRYARKVLTRQLRRVMEADLSLGLAHEALAAIDLG
Ligand information
Ligand IDCAX
InChIInChI=1S/C10H18O3/c1-6-8(11)4-7(5-9(12)13)10(6,2)3/h6-7,9,12-13H,4-5H2,1-3H3/t6-,7+/m1/s1
InChIKeyKAXFPJKKGITBPU-RQJHMYQMSA-N
SMILES
SoftwareSMILES
CACTVS 3.341C[C@@H]1C(=O)C[C@@H](CC(O)O)C1(C)C
OpenEye OEToolkits 1.5.0CC1C(=O)CC(C1(C)C)CC(O)O
ACDLabs 10.04O=C1C(C)C(C)(C)C(CC(O)O)C1
OpenEye OEToolkits 1.5.0C[C@@H]1C(=O)C[C@H](C1(C)C)CC(O)O
CACTVS 3.341C[CH]1C(=O)C[CH](CC(O)O)C1(C)C
FormulaC10 H18 O3
Name(2S,4S)-4-(2,2-DIHYDROXYETHYL)-2,3,3-TRIMETHYLCYCLOPENTANONE;
(2S,4S)-ALPHA-CAMPHOLINIC ACID
ChEMBL
DrugBankDB02906
ZINCZINC000012502823
PDB chain1szo Chain K Residue 5011 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1szo Structure of 6-oxo camphor hydrolase H122A mutant bound to its natural product, (2S,4S)-alpha-campholinic acid: mutant structure suggests an atypical mode of transition state binding for a crotonase homolog.
Resolution1.9 Å
Binding residue
(original residue number in PDB)		W40 H45 F82 W90 I93 H145 D154 E244
Binding residue
(residue number reindexed from 1)		W37 H42 F79 W87 I90 H142 D151 E241
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) I77 F82 I94 Q98 N121 A122 E124 P144 H145 G153 S238
Catalytic site (residue number reindexed from 1) I74 F79 I91 Q95 N118 A119 E121 P141 H142 G150 S235
Enzyme Commision number 3.7.1.18: 6-oxocamphor hydrolase.
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity
GO:0016823 hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances

View graph for
Molecular Function
External links
PDB RCSB:1szo, PDBe:1szo, PDBj:1szo
PDBsum1szo
PubMed15138275
UniProtQ93TU6|CAMK_RHOSO 6-oxocamphor hydrolase (Gene Name=camK)

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