Structure of PDB 2ntk Chain D Binding Site BS01

Receptor Information
>2ntk Chain D (length=202) Species: 145262 (Methanothermobacter thermautotrophicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MYLGRILAVGRNSNGSFVAYRVSSRSFPNRTTSIQEERVAVVPVEGHERD
VFRNPYIAYNCIRIVGDTAVVSNGSHTDTIADKVALGMNLRDAIGLSLLA
MDYEKDELNTPRIAAAINGSEAFIGIVTADGLMVSRVPEETPVYISTYEQ
TEPAATEFKAGSPEEAAEFILKGGEFAAFTHPVTAAAAFNDGEGWNLATR
EM
Ligand information
Ligand IDIMP
InChIInChI=1S/C10H13N4O8P/c15-6-4(1-21-23(18,19)20)22-10(7(6)16)14-3-13-5-8(14)11-2-12-9(5)17/h2-4,6-7,10,15-16H,1H2,(H,11,12,17)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
InChIKeyGRSZFWQUAKGDAV-KQYNXXCUSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.5c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)COP(=O)(O)O)O)O)N=CNC2=O
ACDLabs 10.04O=C1c2ncn(c2N=CN1)C3OC(C(O)C3O)COP(=O)(O)O
OpenEye OEToolkits 1.7.5c1nc2c(n1C3C(C(C(O3)COP(=O)(O)O)O)O)N=CNC2=O
CACTVS 3.385O[CH]1[CH](O)[CH](O[CH]1CO[P](O)(O)=O)n2cnc3C(=O)NC=Nc23
CACTVS 3.385O[C@H]1[C@@H](O)[C@@H](O[C@@H]1CO[P](O)(O)=O)n2cnc3C(=O)NC=Nc23
FormulaC10 H13 N4 O8 P
NameINOSINIC ACID
ChEMBLCHEMBL1207374
DrugBankDB04566
ZINCZINC000004228242
PDB chain2ntk Chain D Residue 208 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2ntk A novel function for the N-terminal nucleophile hydrolase fold demonstrated by the structure of an archaeal inosine monophosphate cyclohydrolase.
Resolution2.03 Å
Binding residue
(original residue number in PDB)		Y2 R5 S24 R25 S26 R30 N54 Y56 Y59 N73 E104 D106 Y148
Binding residue
(residue number reindexed from 1)		Y2 R5 S24 R25 S26 R30 N54 Y56 Y59 N73 E104 D106 Y148
Annotation score4
Enzymatic activity
Enzyme Commision number 3.5.4.10: IMP cyclohydrolase.
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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