Structure of PDB 3gve Chain A

Receptor sequence
>3gveA (length=334) Species: 224308 (Bacillus subtilis subsp. subtilis str. 168) [Search protein sequence]
PQVHLSILATTDIHANMMDYDYYSDKETADFGLARTAQLIQKHREQNPNT
LLVDNGDLIQGNPLGEYAVKYQKDDIISGTKTHPIISVMNALKYDAGTLG
NHEFNYGLDFLDGTIKGADFPIVNANVKTTSGENRYTPYVINEKTLIDEN
GNEQKVKVGYIGFVPPQIMTWDKKNLEGQVQVQDIVESANETIPKMKAEG
ADVIIALAHTGIEKQAQSSGAENAVFDLATKTKGIDAIISGHQHGLFPSA
EYAGVAQFNVEKGTINGIPVVMPSSWGKYLGVIDLKLEKADGSWKVADSK
GSIESIAGNVTSRNETVTNTIQQTHQNTLEYVRK
3D structure
PDB3gve Crystal Structure of Calcineurin-like Phosphoesterase from Bacillus subtilis
ChainA
Resolution1.25 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D16 H18 D61 N105 H106 N109 H213 H246 H248
Catalytic site (residue number reindexed from 1) D12 H14 D57 N101 H102 N105 H209 H242 H244
Enzyme Commision number 3.1.3.5: 5'-nucleotidase.
3.1.3.6: 3'-nucleotidase.
3.1.4.16: 2',3'-cyclic-nucleotide 2'-phosphodiesterase.
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 MN A D16 H18 D61 H248 D12 H14 D57 H244
BS02 MG A D61 N105 H213 H246 D57 N101 H209 H242
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0016787 hydrolase activity
GO:0016788 hydrolase activity, acting on ester bonds
GO:0046872 metal ion binding
Biological Process
GO:0009166 nucleotide catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3gve, PDBe:3gve, PDBj:3gve
PDBsum3gve
PubMed
UniProtO34313|NTPES_BACSU Trifunctional nucleotide phosphoesterase protein YfkN (Gene Name=yfkN)

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