Structure of PDB 5cb5 Chain I

Receptor sequence
>5cb5I (length=173) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
KTRIHVVQGDITKLAVDVIVNAAAPSLMGGGGVAGAIHRAAGPALLDACL
KVRQQQGDCPTGHAVITLAGDLPAKAVVHTVGPVWRGGEQNEDQLLQDAY
LNSLRLVAANSYTSVAFPAISTGVYGYPRAAAAEIAVKTVSEFITRHALP
EQVYFVCYDEENAHLYERLLTQQ
3D structure
PDB5cb5 Structural insights into the mechanism of Escherichia coli YmdB: A 2'-O-acetyl-ADP-ribose deacetylase
ChainI
Resolution2.8 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.1.1.106: O-acetyl-ADP-ribose deacetylase.
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 APR I D11 I12 A23 G32 G33 V34 A120 S122 T123 G124 V125 Y126 Y159 D10 I11 A22 G31 G32 V33 A119 S121 T122 G123 V124 Y125 Y158
Gene Ontology
Molecular Function
GO:0001883 purine nucleoside binding
GO:0008428 ribonuclease inhibitor activity
GO:0016787 hydrolase activity
GO:0019213 deacetylase activity
GO:0019899 enzyme binding
GO:0060698 endoribonuclease inhibitor activity
GO:0061463 O-acetyl-ADP-ribose deacetylase activity
Biological Process
GO:0042278 purine nucleoside metabolic process
GO:0046677 response to antibiotic
GO:0060701 negative regulation of ribonuclease activity
GO:1900231 regulation of single-species biofilm formation on inanimate substrate

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Molecular Function

View graph for
Biological Process
External links
PDB RCSB:5cb5, PDBe:5cb5, PDBj:5cb5
PDBsum5cb5
PubMed26481419
UniProtP0A8D6|YMDB_ECOLI O-acetyl-ADP-ribose deacetylase (Gene Name=ymdB)

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