Structure of PDB 1szo Chain D Binding Site BS01

Receptor Information
>1szo Chain D (length=251) Species: 157732 (Rhodococcus sp. NCIMB 9784) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KQLATPFQEYSQKYENIRLERDGGVLLVTVHTEGKSLVWTSTAHDELAYC
FHDIACDRENKVVILTGTGPSFCNEIDFTSFNLGTPHDWDEIIFEGQRLL
NNLLSIEVPVIAAVNGPVTNAPEIPVMSDIVLAAESATFQDGPHFPSGIV
PGDGAHVVWPHVLGSNRGRYFLLTGQELDARTALDYGAVNEVLSEQELLP
RAWELARGIAEKPLLARRYARKVLTRQLRRVMEADLSLGLAHEALAAIDL
G
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 D Residue 5004 [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 F82 I93 H145 D154 E244
Binding residue
(residue number reindexed from 1)		W39 F81 I92 H144 D153 E243
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) I76 F81 I93 Q97 N120 A121 E123 P143 H144 G152 S237
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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