Structure of PDB 1jf6 Chain B Binding Site BS01

Receptor Information
>1jf6 Chain B (length=585) Species: 2026 (Thermoactinomyces vulgaris) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MLLEAIFHEAKGSYAYPISETQLRVRLRAKKGDVVRCEVLYADRYASPEE
ELAHALAGKAGSDERFDYFEALLECSTKRVKYVFLLTGPQGEAVYFGETG
FSAERSKAGVFQYAYIHRSEVFTTPEWAKEAVIYQIFPERFANGDPSNDP
PGTEQWAKDARPRHDSFYGGDLKGVIDRLPYLEELGVTALYFTPIFASPS
HHKYDTADYLAIDPQFGDLPTFRRLVDEAHRRGIKIILDAVFNHAGDQFF
AFRDVLQKGEQSRYKDWFFIEDFPVSKTSRTNYETYAVQVPAMPKLRTEN
PEVKEYLFDVARFWMEQGIDGWRLDVANEVDHAFWREFRRLVKSLNPDAL
IVGEIWHDASGWLMGDQFDSVMNYLFRESVIRFFATGEIHAERFDAELTR
ARMLYPEQAAQGLWNLLDSHDTERFLTSCGGNEAKFRLAVLFQMTYLGTP
LIYYGDEIGMAGATDPDCRRPMIWEEKEQNRGLFEFYKELIRLRHRLASL
TRGNVRSWHADKQANLYAFVRTVQDQHVGVVLNNRGEKQTVLLQVPESGG
KTWLDCLTGEEVHGKQGQLKLTLRPYQGMILWNGR
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 chain1jf6 Chain B Residue 602 [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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PDB1jf6 Role of Phe286 in the recognition mechanism of cyclomaltooligosaccharides (cyclodextrins) by Thermoactinomyces vulgaris R-47 alpha-amylase 2 (TVAII). X-ray structures of the mutant TVAIIs, F286A and F286Y, and kinetic analyses of the Phe286-replaced mutant TVAIIs
Resolution3.2 Å
Binding residue
(original residue number in PDB)		N143 D145 P146 N148 D149 G169 D171
Binding residue
(residue number reindexed from 1)		N143 D145 P146 N148 D149 G169 D171
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) D239 R323 D325 E354 H420 D421
Catalytic site (residue number reindexed from 1) D239 R323 D325 E354 H420 D421
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1jf6, PDBe:1jf6, PDBj:1jf6
PDBsum1jf6
PubMed11527532
UniProtQ08751|NEPU2_THEVU Neopullulanase 2 (Gene Name=tvaII)

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