Structure of PDB 1up7 Chain E

Receptor sequence
>1up7E (length=406) Species: 243274 (Thermotoga maritima MSB8) [Search protein sequence]
MRIAVIGGGSSYTPELVKGLLDISEDVRIDEVIFYDIDEEKQKIVVDFVK
RLVRFKVLISDTFEGAVVDAKYVIFQFRPGGLKGRENDEGIPLKYGLIGQ
ETTGVGGFSAALRAFPIVEEYVDTVRKTSNATIVNFTNPSGHITEFVRNY
LEYEKFIGLCNVPINFIREIAEMFARLEDVFLKYYGLNHLSFIEKVFVKG
EDVTEKVFENLKLDEDFPTWFYDSVRLIVNPYLRYYLMEKKMFKKISTHE
LRAREVMKIEKELFEKYRTAVEIPEELTKRGGSMYSTAAAHLIRDLETDE
GKIHIVNTRNNGSIENLPDDYVLEIPCYVRSGRVHTLSQGKGDHFALSFI
HAVKMYERLTIEAYLKRSKKLALKALLSHPLGPDVEDAKDLLEEILEANR
EYVKLG
3D structure
PDB1up7 Nad+ and Metal-Ion Dependent Hydrolysis by Family 4 Glycosidases: Structural Insight Into Specificity for Phospho-Beta-D-Glucosides
ChainE
Resolution2.4 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 E S10 Y12 D36 I37 K41 Q78 F79 R80 Y123 F138 N140 G291 Y294 S10 Y12 D36 I37 K41 Q76 F77 R78 Y121 F136 N138 G282 Y285
BS02 G6P E R87 N163 H192 Y241 R261 R289 G290 R85 N161 H189 Y232 R252 R280 G281
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

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

[Back to BioLiP]