Structure of PDB 1szo Chain G

Receptor sequence
>1szoG (length=249) Species: 157732 (Rhodococcus sp. NCIMB 9784) [Search protein sequence]
LATPFQEYSQKYENIRLERDGGVLLVTVHTEGKSLVWTSTAHDELAYCFH
DIACDRENKVVILTGTGPSFCNEIDFTSFNLGTPHDWDEIIFEGQRLLNN
LLSIEVPVIAAVNGPVTNAPEIPVMSDIVLAAESATFQDGPHFPSGIVPG
DGAHVVWPHVLGSNRGRYFLLTGQELDARTALDYGAVNEVLSEQELLPRA
WELARGIAEKPLLARRYARKVLTRQLRRVMEADLSLGLAHEALAAIDLG
3D structure
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.
ChainG
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
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 CAX G W40 F82 H145 D154 E244 W37 F79 H142 D151 E241
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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