Structure of PDB 2ax3 Chain A

Receptor sequence
>2ax3A (length=491) Species: 243274 (Thermotoga maritima MSB8) [Search protein sequence]
HHMKEIDELTIKEYGVDSRILMERAGISVVLAMEEELGNLSDYRFLVLCG
GGNNGGDGFVVARNLLGVVKDVLVVFLGKKKTPDCEYNYGLYKKFGGKVV
EQFEPSILNEFDVVVDAIFGTGLRGEITGEYAEIINLVNKSGKVVVSVDV
PSGIDSNTGKVLRTAVKADLTVTFGVPKIGHILFPGRDLTGKLKVANIGH
PVHLINSINRYVITREMVRSLLPERPRDSHKGTYGKVLIIAGSRLYSGAP
VLSGMGSLKVGTGLVKLAVPFPQNLIATSRFPELISVPIDTEKGFFSLQN
LQECLELSKDVDVVAIGPGLGNNEHVREFVNEFLKTLEKPAVIDADAINV
LDTSVLKERKSPAVLTPHPGEMARLVKKTVGDVKYNYELAEEFAKENDCV
LVLKSATTIVTDGEKTLFNITGNTGLSKGGSGDVLTGMIAGFIAQGLSPL
EASTVSVYLHGFAAELFEQDERGLTASELLRLIPEAIRRLK
3D structure
PDB2ax3 Crystal structure of hypothetical protein (tm0922) from THERMOTOGA MARITIMA at 2.27 A resolution
ChainA
Resolution2.27 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 4.2.1.136: ADP-dependent NAD(P)H-hydrate dehydratase.
5.1.99.6: NAD(P)H-hydrate epimerase.
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 peptide A R22 A30 L191 V193 A194 N195 R24 A32 L193 V195 A196 N197
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016829 lyase activity
GO:0016836 hydro-lyase activity
GO:0016853 isomerase activity
GO:0046872 metal ion binding
GO:0052855 ADP-dependent NAD(P)H-hydrate dehydratase activity
GO:0052856 NAD(P)HX epimerase activity
Biological Process
GO:0046496 nicotinamide nucleotide metabolic process
GO:0110051 metabolite repair

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Molecular Function
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Biological Process
External links
PDB RCSB:2ax3, PDBe:2ax3, PDBj:2ax3
PDBsum2ax3
PubMed
UniProtQ9X024|NNR_THEMA Bifunctional NAD(P)H-hydrate repair enzyme Nnr (Gene Name=nnr)

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