Structure of PDB 2ntk Chain D

Receptor sequence
>2ntkD (length=202) Species: 145262 (Methanothermobacter thermautotrophicus) [Search protein sequence]
MYLGRILAVGRNSNGSFVAYRVSSRSFPNRTTSIQEERVAVVPVEGHERD
VFRNPYIAYNCIRIVGDTAVVSNGSHTDTIADKVALGMNLRDAIGLSLLA
MDYEKDELNTPRIAAAINGSEAFIGIVTADGLMVSRVPEETPVYISTYEQ
TEPAATEFKAGSPEEAAEFILKGGEFAAFTHPVTAAAAFNDGEGWNLATR
EM
3D structure
PDB2ntk A novel function for the N-terminal nucleophile hydrolase fold demonstrated by the structure of an archaeal inosine monophosphate cyclohydrolase.
ChainD
Resolution2.03 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.5.4.10: IMP cyclohydrolase.
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 IMP D Y2 R5 S24 R25 S26 R30 N54 Y56 Y59 N73 E104 D106 Y148 Y2 R5 S24 R25 S26 R30 N54 Y56 Y59 N73 E104 D106 Y148
Gene Ontology
Molecular Function
GO:0003937 IMP cyclohydrolase activity
GO:0016787 hydrolase activity
Biological Process
GO:0006164 purine nucleotide biosynthetic process
GO:0006188 IMP biosynthetic process
GO:0006189 'de novo' IMP biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2ntk, PDBe:2ntk, PDBj:2ntk
PDBsum2ntk
PubMed17407260
UniProtO27099|PURO_METTH IMP cyclohydrolase (Gene Name=purO)

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