Structure of PDB 2hyp Chain A Binding Site BS03

Receptor Information
>2hyp Chain A (length=230) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PRPDYVLLHISDTHLIGGDDADDRLGELLEQLNQSGLRPDAIVFTGDLAA
KGEPAAYRKLRGLVEPFAAQLGAELVWVMGNHDDRAELRKFLLDEAPSMA
PLDRVCMIDGLRIIVLDTSVPGHHHGEIRASQLGWLAEELATPAPDGTIL
ALHHPPIPSVLDMAVTVELRDQAALGRVLRGTDVRAILAGHLHYSTNATF
VGIPVSVASATCGCNLVHVYPDTVVHSVIP
Ligand information
Ligand IDCAC
InChIInChI=1S/C2H7AsO2/c1-3(2,4)5/h1-2H3,(H,4,5)/p-1
InChIKeyOGGXGZAMXPVRFZ-UHFFFAOYSA-M
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.0C[As](=O)(C)[O-]
CACTVS 3.370C[As](C)([O-])=O
ACDLabs 12.01[O-][As](=O)(C)C
FormulaC2 H6 As O2
NameCACODYLATE ION;
dimethylarsinate
ChEMBL
DrugBank
ZINC
PDB chain2hyp Chain A Residue 400 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB2hyp Structural and Biochemical Analysis of the Rv0805 Cyclic Nucleotide Phosphodiesterase from Mycobacterium tuberculosis.
Resolution2.05 Å
Binding residue
(original residue number in PDB)		H23 D63 N97 H98 H207 H209
Binding residue
(residue number reindexed from 1)		H14 D47 N81 H82 H191 H193
Annotation score1
Enzymatic activity
Enzyme Commision number 3.1.4.16: 2',3'-cyclic-nucleotide 2'-phosphodiesterase.
3.1.4.17: 3',5'-cyclic-nucleotide phosphodiesterase.
Gene Ontology
Molecular Function
GO:0004112 cyclic-nucleotide phosphodiesterase activity
GO:0016787 hydrolase activity

View graph for
Molecular Function
External links
PDB RCSB:2hyp, PDBe:2hyp, PDBj:2hyp
PDBsum2hyp
PubMed17059828
UniProtP9WP65|CNPD3_MYCTU cAMP/cGMP dual specificity phosphodiesterase Rv0805 (Gene Name=Rv0805)

[Back to BioLiP]