Structure of PDB 5oke Chain D

Receptor sequence
>5okeD (length=461) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence]
HLKPFPPEFLWGAASAAYQVEGAWNEDGKGLSVWDVFAKQPGRTFKGTNG
DVAVDHYHRYQEDVALMAEMGLKAYRFSVSWSRVFPDGNGAVNEKGLDFY
DRLIEELRNHGIEPIVTLYHWDVPQALMDAYGAWESRRIIDDFDRYAVTL
FQRFGDRVKYWVTLNQQNIFISFGYRLGLHPPGVKDMKRMYEANHIANLA
NAKVIQSFRHYVPDGKIGPSFAYSPMYPYDSRPENVLAFENAEEFQNHWW
MDVYAWGMYPQAAWNYLESQGLEPTVAPGDWELLQAAKPDFMGVNYYQTT
TVEHNPPDGVGTSSGIPGLFKTVRNPHVDTTNWDWAIDPVGLRIGLRRIA
NRYQLPILITENGLGEFDTLEPGDIVNDDYRIDYLRRHVQEIQRAITDGV
DVLGYCAWSFTDLLSWLNGYQKRYGFVYVNRDDESEKDLRRIKKKSFYWY
QRVIETNGAEL
3D structure
PDB5oke Structural basis for enzyme bifunctionality - the case of Gan1D from Geobacillus stearothermophilus.
ChainD
Resolution1.31 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R80 H124 Q170 I173 N299 Y301 E378
Catalytic site (residue number reindexed from 1) R76 H120 Q166 I169 N295 Y297 E361
Enzyme Commision number 3.2.1.85: 6-phospho-beta-galactosidase.
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 BGC D Q170 F177 Y301 Q166 F173 Y297
BS02 BG6 D Q23 H124 Q170 W352 E378 W425 K439 Y441 Q19 H120 Q166 W335 E361 W408 K422 Y424
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0008422 beta-glucosidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0033920 6-phospho-beta-galactosidase activity
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0016052 carbohydrate catabolic process
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5oke, PDBe:5oke, PDBj:5oke
PDBsum5oke
PubMed28975708
UniProtW8QF82

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