Structure of PDB 4ebu Chain A

Receptor sequence
>4ebuA (length=306) Species: 314256 (Oceanicola granulosus HTCC2516) [Search protein sequence]
GVDLGTENLYFQSMMHILSIGECMAELAPADLPGTYRLGFAGDTFNTAWY
LARLRPESRISYFSAIGDDALSQQMRAAMSAAGIDGGGLRVIPGRTVGLY
LITLRSFAYWRGQSAARELAGDADALAAAMARADVVYFSGITLAILDQCG
RATLLRALAQARATGRTIAFDPNLRPRLWAGTGEMTETIMQGAAVSDIAL
PSFEDEAAWFGDAGPDATADRYARAGVRSVVVKNGPHAVHFLQDGRRGRV
PVPPVAQVVDTTAAGDSFNAGLLDSVLAGQPLETAIAAAAALAGQVVQGK
GALVEV
3D structure
PDB4ebu Crystal structure of a sugar kinase (Target EFI-502312) from Oceanicola granulosus, with bound AMP/ADP crystal form I
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) A253 A254 G255 D256
Catalytic site (residue number reindexed from 1) A263 A264 G265 D266
Enzyme Commision number 2.7.1.45: 2-dehydro-3-deoxygluconokinase.
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 ADP A S192 K223 G225 V245 A254 G255 F258 A283 S202 K233 G235 V255 A264 G265 F268 A293
Gene Ontology
Molecular Function
GO:0008673 2-dehydro-3-deoxygluconokinase activity
GO:0016301 kinase activity
GO:0016772 transferase activity, transferring phosphorus-containing groups
GO:0046872 metal ion binding
Biological Process
GO:0006974 DNA damage response
GO:0016310 phosphorylation
GO:0019698 D-galacturonate catabolic process
GO:0042840 D-glucuronate catabolic process
GO:0046835 carbohydrate phosphorylation
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Cellular Component
External links
PDB RCSB:4ebu, PDBe:4ebu, PDBj:4ebu
PDBsum4ebu
PubMed
UniProtQ2CIP5

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