Structure of PDB 5okg Chain C

Receptor sequence
>5okgC (length=462) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence]
RHLKPFPPEFLWGAASAAYQVEGAWNEDGKGLSVWDVFAKQPGRTFKGTN
GDVAVDHYHRYQEDVALMAEMGLKAYRFSVSWSRVFPDGNGAVNEKGLDF
YDRLIEELRNHGIEPIVTLYHWDVPQALMDAYGAWESRRIIDDFDRYAVT
LFQRFGDRVKYWVTLNQQNIFISFGYRLGLHPPGVKDMKRMYEANHIANL
ANAKVIQSFRHYVPDGKIGPSFAYSPMYPYDSRPENVLAFENAEEFQNHW
WMDVYAWGMYPQAAWNYLESQGLEPTVAPGDWELLQAAKPDFMGVNYYQT
TTVEHNPPDGVGTSSGIPGLFKTVRNPHVDTTNWDWAIDPVGLRIGLRRI
ANRYQLPILITENGLGEFDTLEPGDIVNDDYRIDYLRRHVQEIQRAITDG
VDVLGYCAWSFTDLLSWLNGYQKRYGFVYVNRDDESEKDLRRIKKKSFYW
YQRVIETNGAEL
3D structure
PDB5okg Structural basis for enzyme bifunctionality - the case of Gan1D from Geobacillus stearothermophilus.
ChainC
Resolution1.25 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) R77 H121 Q167 I170 N296 Y298 E362
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 C Q170 Y301 Q167 Y298
BS02 BG6 C Q23 H124 Q170 E378 W425 S432 W433 Y441 Q20 H121 Q167 E362 W409 S416 W417 Y425
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:5okg, PDBe:5okg, PDBj:5okg
PDBsum5okg
PubMed28975708
UniProtW8QF82

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