Structure of PDB 1up7 Chain B

Receptor sequence
>1up7B (length=409) Species: 243274 (Thermotoga maritima MSB8) [Search protein sequence]
MRIAVIGGGSSYTPELVKGLLDISEDVRIDEVIFYDIDEEKQKIVVDFVK
RLVKDRFKVLISDTFEGAVVDAKYVIFQFRPGGLKGRENDEGIPLKYGLI
GQETTGVGGFSAALRAFPIVEEYVDTVRKTSNATIVNFTNPSGHITEFVR
NYLEYEKFIGLCNVPINFIREIAEMFSARLEDVFLKYYGLNHLSFIEKVF
VKGEDVTEKVFENLKLKEDFPTWFYDSVRLIVNPYLRYYLMEKKMFKKIS
THELRAREVMKIEKELFEKYRTAVEIPEELTKRGGSMYSTAAAHLIRDLE
TDEGKIHIVNTRNNGSIENLPDDYVLEIPCYVRSGRVHTLSQGKGDHFAL
SFIHAVKMYERLTIEAYLKRSKKLALKALLSHPLGPDVEDAKDLLEEILE
ANREYVKLG
3D structure
PDB1up7 Nad+ and Metal-Ion Dependent Hydrolysis by Family 4 Glycosidases: Structural Insight Into Specificity for Phospho-Beta-D-Glucosides
ChainB
Resolution2.4 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.86: 6-phospho-beta-glucosidase.
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 NAD B G9 S10 Y12 D36 I37 K41 Q78 F79 R80 Y123 F138 N140 R289 G291 Y294 G9 S10 Y12 D36 I37 K41 Q78 F79 R80 Y123 F138 N140 R283 G285 Y288
BS02 G6P B R87 E103 N163 H192 Y241 R261 R289 G290 Y294 R87 E103 N163 H192 Y235 R255 R283 G284 Y288
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0008706 6-phospho-beta-glucosidase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1up7, PDBe:1up7, PDBj:1up7
PDBsum1up7
PubMed15670594
UniProtQ9X108|BGLT_THEMA 6-phospho-beta-glucosidase BglT (Gene Name=bglT)

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