Structure of PDB 2c40 Chain B

Receptor sequence
>2c40B (length=300) Species: 198094 (Bacillus anthracis str. Ames) [Search protein sequence]
MKKVYFNHDGGVDDLVSLFLLLQMDNVELTGVSVIPADCYLEPAMSASRK
IIDRFGKNTIEVAASNSRGKNPFPKDWRMHAFYVDALPILNESGKVVTHV
AAKPAHHHLIETLLQTEEKTTLLFTGPLTDLARALYEAPIIENKIKRLVW
MGGTFRTAGNVHEPEHDGTAEWNSFWDPEAVARVWEANIEIDLITLESTN
QVPLTIDIREQWAKERKYIGIDFLGQCYAIVPPYLWDVLTAAFVGKADLA
KVQTINSIVHTYGPSQGRTVETDDGRPVHVVYDVNHDRFFDYITRLAKKV
3D structure
PDB2c40 Crystal Structure of Inosine-Uridine Preferring Nucleoside Hydrolase from Bacillus Anthracis at 2.2A Resolution
ChainB
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D9 D14 D38 W77 T125 W172 N173 W246 D247
Catalytic site (residue number reindexed from 1) D9 D14 D38 W77 T125 W172 N173 W236 D237
Enzyme Commision number 3.2.2.1: purine nucleosidase.
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 CA B D9 D14 T125 D247 D9 D14 T125 D237
BS02 RIB B D38 F73 N160 E171 N173 D247 D38 F73 N160 E171 N173 D237
Gene Ontology
Molecular Function
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0016799 hydrolase activity, hydrolyzing N-glycosyl compounds
GO:0046872 metal ion binding
Biological Process
GO:0006139 nucleobase-containing compound metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2c40, PDBe:2c40, PDBj:2c40
PDBsum2c40
PubMed
UniProtQ81QM4

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