Structure of PDB 2yb1 Chain A Binding Site BS03

Receptor Information
>2yb1 Chain A (length=284) Species: 536 (Chromobacterium violaceum) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ANIDLHFHSRTSDGALTPTEVIDRAAARAPALLALTDHDCTGGLAEAAAA
AARRGIPFLNGVEVSVSWGRHTVHIVGLGIDPAEPALAAGLKSIREGRLE
RARQMGASLEAAGIAGCFDGAMRWCDNPEMISRTHFARHLVDSGAVKDMR
TVFRKYLTPGKPGYVSHQWASLEDAVGWIVGAGGMAVIAHPGRYDMGRTL
IERLILDFQAAGGQGIEVASGSHSLDDMHKFALHADRHGLYASSGSDFHA
PGEDVGHTEDLPPICRPIWRELEARILRPADAEN
Ligand information
Ligand IDMN
InChIInChI=1S/Mn/q+2
InChIKeyWAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mn+2]
CACTVS 3.341[Mn++]
FormulaMn
NameMANGANESE (II) ION
ChEMBL
DrugBankDB06757
ZINC
PDB chain2yb1 Chain A Residue 1291 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2yb1 Prospecting for Unannotated Enzymes: Discovery of a 3',5'-Nucleotide Bisphosphate Phosphatase within the Amidohydrolase Superfamily.
Resolution1.898 Å
Binding residue
(original residue number in PDB)		E64 H75 H191
Binding residue
(residue number reindexed from 1)		E63 H74 H190
Annotation score1
Enzymatic activity
Enzyme Commision number 3.1.3.97: 3',5'-nucleoside bisphosphate phosphatase.
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003824 catalytic activity
GO:0004534 5'-3' RNA exonuclease activity
GO:0016787 hydrolase activity
GO:0030145 manganese ion binding
GO:0035312 5'-3' DNA exonuclease activity
GO:0046872 metal ion binding
GO:0097657 3',5'-nucleotide bisphosphate phosphatase activity
Biological Process
GO:0006259 DNA metabolic process
GO:0016311 dephosphorylation

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Molecular Function
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Biological Process
External links
PDB RCSB:2yb1, PDBe:2yb1, PDBj:2yb1
PDBsum2yb1
PubMed24401123
UniProtQ7NXD4|35NBP_CHRVO 3',5'-nucleoside bisphosphate phosphatase (Gene Name=CV_1693)

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