Structure of PDB 3gbe Chain A

Receptor sequence
>3gbeA (length=558) [Search protein sequence]
TIPKWWKEAVFYQVYPRSFKDTNGDGIGDINGIIEKLDYLKALGIDAIWI
NPHYDSPNTDNGYDIRDYRKIMKEYGTMEDFDRLISEMKKRNMRLMIDVV
INHTSDQNEWFVKSKSSKDNPYRGYYFWKDAKEGQAPNNYPSFFGGSAWQ
KDEKTNQYYLHYFAKQQPDLNWDNPKVRQDLYAMLRFWLDKGVSGLRFDT
VATYSKIPDFPNLTQQQLKNFAAEYTKGPNIHRYVNEMNKEVLSHYDIAT
AGEIFGVPLDQSIKFFDRRRDELNIAFTFDLIRLDRDSDQRWRRKDWKLS
QFRQIIDNVDRTAGEYGWNAFFLDNHDNPRAVSHFGDDRPQWREPSAKAL
ATLTLTQRATPFIYQGSELGMTNYPFKAIDEFDDIEVKGFWHDYVETGKV
KADEFLQNVRLTSRDNSRTPFQWDGSKNAGFTSGKPWFKVNPNYQEINAV
SQVTQPDSVFNYYRQLIKIRHDIPALTYGTYTDLDPANDSVYAYTRSLGA
EKYLVVVNFKEQMMRYKLPDNLSIEKVIIDSNSKNVVKKNDSLLELKPWQ
SGVYKLNQ
3D structure
PDB3gbe Structural determinants of product specificity of sucrose isomerases
ChainA
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D113 R212 D214 E268 H341 D342
Catalytic site (residue number reindexed from 1) D98 R197 D199 E253 H326 D327
Enzyme Commision number 5.4.99.11: isomaltulose synthase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 NOJ A D75 Y78 H118 F178 R212 D214 H341 D342 R429 D60 Y63 H103 F163 R197 D199 H326 D327 R414 MOAD: Ki=10uM
PDBbind-CN: -logKd/Ki=5.00,Ki=10uM
Gene Ontology
Molecular Function
GO:0004556 alpha-amylase activity
GO:0050006 isomaltulose synthase activity
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0009313 oligosaccharide catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3gbe, PDBe:3gbe, PDBj:3gbe
PDBsum3gbe
PubMed19427862
UniProtD0VX20

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