Structure of PDB 1uh2 Chain A Binding Site BS09

Receptor Information
>1uh2 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
DGWRLNAAQYVDANGNNGSDVTNHQIWSEFRNAVKGVNSNAAIIGQYWGN
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 chain1uh2 Chain A Residue 1001 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1uh2 Complex Structures of Thermoactinomyces vulgaris R-47 alpha-Amylase 1 with Malto-oligosaccharides Demonstrate the Role of Domain N Acting as a Starch-binding Domain
Resolution2.0 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 Q396 H471 D472
Catalytic site (residue number reindexed from 1) D262 R354 N356 Q396 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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1uh2, PDBe:1uh2, PDBj:1uh2
PDBsum1uh2
PubMed14687576
UniProtQ60053|NEPU1_THEVU Neopullulanase 1 (Gene Name=tvaI)

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