Structure of PDB 2dte Chain A

Receptor sequence
>2dteA (length=255) Species: 2303 (Thermoplasma acidophilum) [Search protein sequence]
GFSDLRDKVVIVTGASMGIGRAIAERFVDEGSKVIDLSIHDPGEAKYDHI
ECDVTNPDQVKASIDHIFKEYGSISVLVNNAGIESYGKIESMSMGEWRRI
IDVNLFGYYYASKFAIPYMIRSRDPSIVNISSVQASIITKNASAYVTSKH
AVIGLTKSIALDYAPLLRCNAVCPATIDTPLVRKAAELEVGSDPMRIEKK
ISEWGHEHPMQRIGKPQEVASAVAFLASREASFITGTCLYVDGGLSIRAP
ISTPE
3D structure
PDB2dte Structural Insights into Unique Substrate Selectivity of Thermoplasma acidophilumd-Aldohexose Dehydrogenase
ChainA
Resolution1.65 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) G18 S132 Y145 S148 K149
Catalytic site (residue number reindexed from 1) G18 S132 Y145 S148 K149
Enzyme Commision number 1.1.1.118: glucose 1-dehydrogenase (NAD(+)).
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 NAI A G14 S16 M17 G18 I19 S38 I39 C52 D53 V54 N80 A81 I130 S132 Y145 K149 P174 A175 T176 I177 T179 P180 L181 V182 G14 S16 M17 G18 I19 S38 I39 C52 D53 V54 N80 A81 I130 S132 Y145 K149 P174 A175 T176 I177 T179 P180 L181 V182
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0016491 oxidoreductase activity

View graph for
Molecular Function
External links
PDB RCSB:2dte, PDBe:2dte, PDBj:2dte
PDBsum2dte
PubMed17300803
UniProtQ9HK51

[Back to BioLiP]