Structure of PDB 5okb Chain B

Receptor sequence
>5okbB (length=474) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence]
HLKPFPPEFLWGAASAAYQVEGAWNEDGKGLSVWDVFAKQPGRTFKGTNG
DVAVDHYHRYQEDVALMAEMGLKAYRFSVSWSRVFPDGNGAVNEKGLDFY
DRLIEELRNHGIEPIVTLYHWDVPQALMDAYGAWESRRIIDDFDRYAVTL
FQRFGDRVKYWVTLNEQNIFISFGYRLGLHPPGVKDMKRMYEANHIANLA
NAKVIQSFRHYVPDGKIGPSFAYSPMYPYDSRPENVLAFENAEEFQNHWW
MDVYAWGMYPQAAWNYLESQGLEPTVAPGDWELLQAAKPDFMGVNYYQTT
TVEHNPPDGVGEGVMNTTGKKGTSTSSGIPGLFKTVRNPHVDTTNWDWAI
DPVGLRIGLRRIANRYQLPILITENGLGEFDTLEPGDIVNDDYRIDYLRR
HVQEIQRAITDGVDVLGYCAWSFTDLLSWLNGYQKRYGFVYVNRDDESEK
DLRRIKKKSFYWYQRVIETNGAEL
3D structure
PDB5okb Structural basis for enzyme bifunctionality - the case of Gan1D from Geobacillus stearothermophilus.
ChainB
Resolution1.331 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 E170 I173 N299 Y301 E378
Catalytic site (residue number reindexed from 1) R76 H120 E166 I169 N295 Y297 E374
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 PO4 B S432 K439 Y441 S428 K435 Y437
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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Cellular Component
External links
PDB RCSB:5okb, PDBe:5okb, PDBj:5okb
PDBsum5okb
PubMed28975708
UniProtW8QF82

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