Structure of PDB 1bhg Chain A

Receptor sequence
>1bhgA (length=611) Species: 9606 (Homo sapiens) [Search protein sequence]
GLQGGMLYPQESPSRECKELDGLWSFRADFSDNRRRGFEEQWYRRPLWES
GPTVDMPVPSSFNDISQDWRLRHFVGWVWYEREVILPERWTQDLRTRVVL
RIGSAHSYAIVWVNGVDTLEHEGGYLPFEADISNLVQVGPLPSRLRITIA
INNTLTPTTLPPGTIQYLTDTSKYPKGYFVQNTYFDFFNYAGLQRSVLLY
TTPTTYIDDITVTTSVEQDSGLVNYQISVKGSNLFKLEVRLLDAENKVVA
NGTGTQGQLKVPGVSLWWPYLMHERPAYLYSLEVQLTAQTSLGPVSDFYT
LPVGIRTVAVTKSQFLINGKPFYFHGVNKHEDADIRGKGFDWPLLVKDFN
LLRWLGANAFRTSHYPYAEEVMQMCDRYGIVVIDECPGVGLALPQFFNNV
SLHHHMQVMEEVVRRDKNHPAVVMWSVANEPASHLESAGYYLKMVIAHTK
SLDPSRPVTFVSNSNYAADKGAPYVDVICLNSYYSWYHDYGHLELIQLQL
ATQFENWYKKYQKPIIQSEYGAETIAGFHQDPPLMFTEEYQKSLLEQYHL
GLDQKRRKYVVGELIWNFADFMTEQSPTRVLGNKKGIFTRQRQPKSAAFL
LRERYWKIANE
3D structure
PDB1bhg Structure of human beta-glucuronidase reveals candidate lysosomal targeting and active-site motifs.
ChainA
Resolution2.53 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D207 H351 H385 V410 L412 E451 Y504 E540 K606
Catalytic site (residue number reindexed from 1) D186 H330 H364 V389 L391 E430 Y483 E519 K585
Enzyme Commision number 3.2.1.31: beta-glucuronidase.
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 MAN A K197 G198 K176 G177
BS02 MAN A T185 Q187 T164 Q166
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1bhg, PDBe:1bhg, PDBj:1bhg
PDBsum1bhg
PubMed8599764
UniProtP08236|BGLR_HUMAN Beta-glucuronidase (Gene Name=GUSB)

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