Structure of PDB 2d0f Chain A Binding Site BS07

Receptor Information
>2d0f Chain A (length=637) Species: 2026 (Thermoactinomyces vulgaris) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AANDNNVEWNGLFHDQGPLFDNAPEPTSTQSVTLKLRTFKGDITSANIKY
WDTADNAFHWVPMVWDSNDPTGTFDYWKGTIPASPSIKYYRFQINDGTST
AWYNGNGPSSTEPNADDFYIIPNFKTPDWLKNGVMYQIFPDRFYNGDSSN
DVQTGSYTYNGTPTEKKAWGSSVYADPGYDNSLVFFGGDLAGIDQKLGYI
KKTLGANILYLNPIFKAPTNHKYDTQDYMAVDPAFGDNSTLQTLINDIHS
TANGPKGYLILDGVFNHTGDSHPWFDKYNNFSSQGAYESQSSPWYNYYTF
YTWPDSYASFLGFNSLPKLNYGNSGSAVRGVIYNNSNSVAKTYLNPPYSV
DGWRLNAAQYVDANGNNGSDVTNHQIWSEFRNAVKGVNSNAAIIGEYWGN
ANPWTAQGNQWDAATNFDGFTQPVSEWITGKDYQNNSASISTTQFDSWLR
GTRANYPTNVQQSMMNFLSNHDITRFATRSGGDLWKTYLALIFQMTYVGT
PTIYYGDEYGMQGGADPDNRRSFDWSQATPSNSAVALTQKLITIRNQYPA
LRTGSFMTLITDDTNKIYSYGRFDNVNRIAVVLNNDSVSHTVNVPVWQLS
MPNGSTVTDKITGHSYTVQNGMVTVAVDGHYGAVLAQ
Ligand information
Ligand IDCA
InChIInChI=1S/Ca/q+2
InChIKeyBHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Ca+2]
FormulaCa
NameCALCIUM ION
ChEMBL
DrugBankDB14577
ZINC
PDB chain2d0f Chain A Residue 2001 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB2d0f Complexes of Thermoactinomyces vulgaris R-47 alpha-amylase 1 and pullulan model oligossacharides provide new insight into the mechanism for recognizing substrates with alpha-(1,6) glycosidic linkages
Resolution2.08 Å
Binding residue
(original residue number in PDB)		A2 D4 N6 D42 D96
Binding residue
(residue number reindexed from 1)		A2 D4 N6 D42 D96
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) D262 R354 N356 E396 H471 D472
Catalytic site (residue number reindexed from 1) D262 R354 N356 E396 H471 D472
Enzyme Commision number 3.2.1.135: neopullulanase.
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0031216 neopullulanase activity
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
Cellular Component
GO:0005576 extracellular region

View graph for
Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2d0f, PDBe:2d0f, PDBj:2d0f
PDBsum2d0f
PubMed16302977
UniProtQ60053|NEPU1_THEVU Neopullulanase 1 (Gene Name=tvaI)

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