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BioLiP

Structure of PDB 1odt Chain C

Receptor sequence
>1odtC (length=317) Species: 1423 (Bacillus subtilis) [Search protein sequence]
MQLFDLPLDQLQTYKPEKTAPKDFSEFWKLSLEELAKVQAEPDLQPVDYP
ADGVKVYRLTYKSFGNARITGWYAVPDKEGPHPAIVKYHGYNASYDGEIH
EMVNWALHGYATFGMLVRGQQSSEDTSISPHGHALGWMTKGILDKDTYYY
RGVYLDAVRALEVISSFDEVDETRIGVTGGAQGGGLTIAAAALSDIPKAA
VADYPYLSNFERAIDVALEEPYLEINSFFRRNGSPETEVQAMKTLSYFDI
MNLADRVKVPVLMSIGLIDKVTPPSTVFAAYNHLETKKELKVYRYFGHEY
IPAFQTEKLAFFKQHLK
3D structure
PDB1odt Multifunctional Xylooligosaccharide/Cephalosporin C Deacetylase Revealed by the Hexameric Structure of the Bacillus Subtilis Enzyme at 1.9A Resolution
ChainC
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y91 A181 Q182 D269 H298
Catalytic site (residue number reindexed from 1) Y91 A181 Q182 D269 H298
Enzyme Commision number 3.1.1.41: cephalosporin-C deacetylase.
3.1.1.72: acetylxylan esterase.
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 ACT C G90 Y91 A181 Q182 Y206 P221 H298 G90 Y91 A181 Q182 Y206 P221 H298
Gene Ontology
Molecular Function
GO:0016788 hydrolase activity, acting on ester bonds
GO:0046555 acetylxylan esterase activity
GO:0047739 cephalosporin-C deacetylase activity
GO:0052689 carboxylic ester hydrolase activity
Biological Process
GO:0005976 polysaccharide metabolic process
GO:0030245 cellulose catabolic process
Cellular Component
GO:0005737 cytoplasm

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Cellular Component
External links
PDB RCSB:1odt, PDBe:1odt, PDBj:1odt
PDBsum1odt
PubMed12842474
UniProtP94388|CAH_BACSU Cephalosporin-C deacetylase (Gene Name=cah)

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