Structure of PDB 1odt Chain H

Receptor sequence
>1odtH (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
ChainH
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 H 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

View graph for
Molecular Function

View graph for
Biological Process

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

[Back to BioLiP]