Structure of PDB 1izj Chain A Binding Site BS02

Receptor Information
>1izj 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
YTWPDSYASFLGANSLPKLNYGNSGSAVRGVIYNNSNSVAKTYLNPPYSV
DGWRLDAAQYVDANGNNGSDVTNHQIWSEFRNAVKGVNSNAAIIGEYWGN
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 chain1izj Chain A Residue 1002 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1izj Mutual conversion of substrate specificities of Thermoactinomyces vulgaris R-47 alpha-amylases TVAI and TVAII by site-directed mutagenesis
Resolution2.2 Å
Binding residue
(original residue number in PDB)		D276 N279 F281 S283 E288
Binding residue
(residue number reindexed from 1)		D276 N279 F281 S283 E288
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) D262 R354 D356 E396 H471 D472
Catalytic site (residue number reindexed from 1) D262 R354 D356 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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1izj, PDBe:1izj, PDBj:1izj
PDBsum1izj
PubMed12860426
UniProtQ60053|NEPU1_THEVU Neopullulanase 1 (Gene Name=tvaI)

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