Structure of PDB 3tto Chain C Binding Site BS01

Receptor Information
>3tto Chain C (length=1052) Species: 1245 (Leuconostoc mesenteroides) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KGLRQDSNGKLRYFDLTTGIQAKGQFVTIGQETYYFSKDHGDAQLLPMVT
EGHYGTITLKQGQDTKTAWVYRDQNNTILKGLQNINGTLQFFDPYTGEQL
KGGVAKYDDKLFYFESGKGNLVSTVAGDYQDGHYISQDGQTRYADKQNQL
VKGLVTVNGALQYFDNATGNQIKNQQVIVDGKTYYFDDKGNGEYLFTNTL
DMSTNAFSTKNVAFNHDSSSFDHTVDGFLTADTWYRPKSILANGTTWRDS
TDKDMRPLITVWWPNKNVQVNYLNFMKANGLLTTAAQYTLHSDQYDLNQA
AQDVQVAIERRIASEHGTDWLQKLLFESQNNNPSFVKQQFIWNKDSEYHG
GGDAWFQGGYLKYGNNPLTPTTNSDYRQPGNAFDFLLANDVDNSNPVVQA
ENLNWLHYLMNFGTITAGQDDANFDSIRIDAVDFIHNDTIQRTYDYLRDA
YQVQQSEAKANQHISLVEAGLDAGTSTIHNDALIESNLREAATLSLTNEP
GKNKPLTNMLQDVDGGTLITDHTQNSTENQATPNYSIIHAHDKGVQEKVG
AAITDATGADWTNFTDEQLKAGLELFYKDQRATNKKYNSYNIPSIYALML
TNKDTVPRMYYGDMYQDDGQYMANKSIYYDALVSLMTARKSYVSGGQTMS
VDNHGLLKSVRFGKDAMTANDLGTSATRTEGLGVIIGNDPKLQLNDSDKV
TLDMGAAHKNQKYRAVILTTRDGLATFNSDQAPTAWTNDQGTLTFSNQEI
NGQDNTQIRGVANPQVSGYLAVWVPVGASDNQDARTAATTTENHDGKVLH
SNAALDSNLIYEGFSNFQPKATTHDELTNVVIAKNADVFNNWGITSFEMA
PQYRSSGDHTFLDSTIDNGYAFTDRYDLGFNTPTKYGTDGDLRATIQALH
HANMQVMADVVDNQVYNLPGKEVVSATRAGVYGNDDATGFGTQLYVTNSV
GGGQYQEKYAGQYLEALKAKYPDLFEGKAYDYWYKNYANDGSNPYYTLSH
GDRESIPADVAIKQWSAKYMNGTNVLGNGMGYVLKDWHNGQYFKLDGDKS
TL
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 chain3tto Chain C Residue 2866 [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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PDB3tto Functional and structural characterization of alpha-(1-2) branching sucrase derived from DSR-E glucansucrase
Resolution3.3 Å
Binding residue
(original residue number in PDB)		D2164 D2170 F2214 N2693
Binding residue
(residue number reindexed from 1)		D384 D390 F434 N913
Annotation score1
Enzymatic activity
Enzyme Commision number 2.4.1.5: dextransucrase.
Gene Ontology
Molecular Function
GO:0046527 glucosyltransferase activity
Biological Process
GO:0009250 glucan biosynthetic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3tto, PDBe:3tto, PDBj:3tto
PDBsum3tto
PubMed22262856
UniProtQ8G9Q2

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