Structure of PDB 1v1a Chain A

Receptor sequence
>1v1aA (length=301) Species: 300852 (Thermus thermophilus HB8) [Search protein sequence]
MLEVVTAGEPLVALVPQEPGHLRGKRLLEVYVGGAEVNVAVALARLGVKV
GFVGRVGEDELGAMVEERLRAEGVDLTHFRRAPGFTGLYLREYLPLGQGR
VFYYRKGSAGSALAPGAFDPDYLEGVRFLHLSGITPALSPEARAFSLWAM
EEAKRRGVRVSLDVNYRQTLWSPEEARGFLERALPGVDLLFLSEEEAELL
FGRVEEALRALSAPEVVLKRGAKGAWAFVDGRRVEGSAFAVEAVDPVGAG
DAFAAGYLAGAVWGLPVEERLRLANLLGASVAASRGDHEGAPYREDLEVL
L
3D structure
PDB1v1a Structure of Thermus thermophilus 2-Keto-3-deoxygluconate kinase: evidence for recognition of an open chain substrate.
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G248 A249 G250 D251
Catalytic site (residue number reindexed from 1) G248 A249 G250 D251
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 KDG A L11 G34 A35 N38 Y89 R105 R167 G248 D251 D287 L11 G34 A35 N38 Y89 R105 R167 G248 D251 D287
BS02 ADP A K219 G221 A222 A249 G250 N275 A279 K219 G221 A222 A249 G250 N275 A279
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0005524 ATP binding
GO:0008673 2-dehydro-3-deoxygluconokinase activity
GO:0016301 kinase activity
GO:0016772 transferase activity, transferring phosphorus-containing groups
Biological Process
GO:0016310 phosphorylation
GO:0046835 carbohydrate phosphorylation

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1v1a, PDBe:1v1a, PDBj:1v1a
PDBsum1v1a
PubMed15210349
UniProtQ53W83|KDGK_THET8 2-dehydro-3-deoxygluconokinase (Gene Name=kdgK)

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