Structure of PDB 1ons Chain A

Receptor sequence
>1onsA (length=278) Species: 562 (Escherichia coli) [Search protein sequence]
TSKNPQVDIAEDNAFFPSEYSLSQYTSPVSDLDGVDYPKPYRGKHKILVI
AADERYLPTDNGKLFSTGNHPIETLLPLYHLHAAGFEFEVATISGLMTKF
EYWAMPHKDEKVMPFFEQHKSLFRNPKKLADVVASLNADSEYAAIFVPGG
HGALIGLPESQDVAAALQWAIKNDRFVISLCHGPAAFLALRHGDNPLNGY
SICAFPDAADKQTPEIGYMPGHLTWYFGEELKKMGMNIINDDITGRVHKD
RKLLTGDSPFAANALGKLAAQEMLAAYA
3D structure
PDB1ons The crystal structure of Escherichia coli heat shock protein YedU reveals three potential catalytic active sites
ChainA
Resolution2.2 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.1.2.-
3.5.1.-
3.5.1.124: protein deglycase.
4.2.1.130: D-lactate dehydratase.
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 ZN A H85 E90 H122 H82 E87 H119
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0008270 zinc ion binding
GO:0016787 hydrolase activity
GO:0016790 thiolester hydrolase activity
GO:0016829 lyase activity
GO:0019172 glyoxalase III activity
GO:0036524 protein deglycase activity
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
Biological Process
GO:0006281 DNA repair
GO:0010447 response to acidic pH
GO:0019243 methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione
GO:0019249 lactate biosynthetic process
GO:0030091 protein repair
GO:0042245 RNA repair
GO:0051595 response to methylglyoxal
GO:0106044 guanine deglycation
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:1ons, PDBe:1ons, PDBj:1ons
PDBsum1ons
PubMed14500888
UniProtP31658|HCHA_ECOLI Protein/nucleic acid deglycase 1 (Gene Name=hchA)

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